4.5 Article

Structural and functional characterization of Helicobacter pylori DsbG

Journal

FEBS LETTERS
Volume 585, Issue 24, Pages 3862-3867

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2011.10.042

Keywords

Disulfide bond; DsbG; HP0231; HP0518; Reductase activity; Helicobacter pylori

Funding

  1. Korea Ministry of Education, Science, and Technology
  2. National Research Foundation of Korea
  3. Innovative Drug Research Center for Metabolic and Inflammatory Disease [R11-2007-107-00000-0]
  4. Basic Science Outstanding Scholars Program
  5. WorldClass University Program
  6. Korea Healthcare Technology RD Project
  7. Ministry of Health, Welfare & Family Affairs, Republic of Korea [A092006]

Ask authors/readers for more resources

Dsb proteins play important roles in bacterial pathogenicity. To better understand the role of Dsb proteins in Helicobacter pylori, we have structurally and functionally characterized H. pylori DsbG (HP0231). The monomer consists of two domains connected by a helical linker. Two monomers associate to form a V-shaped dimer. The monomeric and dimeric structures of H. pylori DsbG show significant differences compared to Escherichia coli DsbG. Two polyethylene glycol molecules are bound in the cleft of the V-shaped dimer, suggesting a possible role as a chaperone. Furthermore, we show that H. pylori DsbG functions as a reductase against HP0518, a putative L, D-transpeptidase with a catalytic cysteine residue. Structured summary of protein interactions: DsbG and DsbG bind by X-ray crystallography (View interaction). (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

Article Biochemistry & Molecular Biology

Structural changes of antitoxin HigA from Shigella flexneri by binding of its cognate toxin HigB

Won-Su Yoon, Seung-Hyeon Seok, Hyung-Sik Won, Taehwan Cho, Sang Jae Lee, Min-Duk Seo

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES (2019)

Article Multidisciplinary Sciences

Nylon mesh-based sample holder for fixed-target serial femtosecond crystallography

Donghyeon Lee, Sangwon Baek, Jaehyun Park, Keondo Lee, Jangwoo Kim, Sang Jae Lee, Wan Kyun Chung, Jong-Lam Lee, Yunje Cho, Ki Hyun Nam

SCIENTIFIC REPORTS (2019)

Article Multidisciplinary Sciences

A host dTMP-bound structure of T4 phage dCMP hydroxymethylase mutant using an X-ray free electron laser

Si Hoon Park, Jaehyun Park, Sang Jae Lee, Woo Seok Yang, Sehan Park, Kyungdo Kim, Zee-Yong Park, Hyun Kyu Song

SCIENTIFIC REPORTS (2019)

Article Biochemistry & Molecular Biology

Crystal structures of human NSDHL and development of its novel inhibitor with the potential to suppress EGFR activity

Dong-Gyun Kim, Sujin Cho, Kyu-Yeon Lee, Seung-Ho Cheon, Hye-Jin Yoon, Joo-Youn Lee, Dongyoon Kim, Kwang-Soo Shin, Choong-Hyun Koh, Ji Sung Koo, Yuri Choi, Hyung Ho Lee, Yu-Kyoung Oh, Yoo-Seong Jeong, Suk-Jae Chung, Moonkyu Baek, Kwan-Young Jung, Hyo Jin Lim, Hyoun Sook Kim, Sung Jean Park, Jeong-Yeon Lee, Sang Jae Lee, Bong-Jin Lee

Summary: NSDHL, a crucial enzyme in human cholesterol synthesis and regulator of EGFR, has been studied for its potential therapeutic applications. Two X-ray crystal structures of human NSDHL were reported, revealing coenzyme-binding details and a conformational change. A novel inhibitor for NSDHL was identified, showing suppressive activity towards EGFR, enhancing antitumor effects in EGFR-driven cancer cells. These findings may serve as a platform for developing therapeutic agents against NSDHL-related diseases.

CELLULAR AND MOLECULAR LIFE SCIENCES (2021)

Article Biochemistry & Molecular Biology

Crystal structure of proteolyzed VapBC and DNA-bound VapBC from Salmonella enterica Typhimurium LT2 and VapC as a putative Ca2+-dependent ribonuclease

DongWon Park, Hye-Jin Yoon, Ki-Young Lee, Sung-Jean Park, Seung-Ho Cheon, Hyung Ho Lee, Sang Jae Lee, Bong-Jin Lee

FASEB JOURNAL (2020)

Article Chemistry, Multidisciplinary

A structural study of TatD from Staphylococcus aureus elucidates a putative DNA-binding mode of a Mg2+-dependent nuclease

Kyu-Yeon Lee, Seung-Ho Cheon, Dong-Gyun Kim, Sang Jae Lee, Bong-Jin Lee

IUCRJ (2020)

Article Chemistry, Multidisciplinary

High-Resolution XFEL Structure of the Soluble Methane Monooxygenase Hydroxylase Complex with its Regulatory Component at Ambient Temperature in Two Oxidation States

Vivek Srinivas, Rahul Banerjee, Hugo Lebrette, Jason C. Jones, Oskar Aurelius, In-Sik Kim, Cindy C. Pham, Sheraz Gul, Kyle D. Sutherlin, Asmit Bhowmick, Juliane John, Esra Bozkurt, Thomas Fransson, Pierre Aller, Agata Butryn, Isabel Bogacz, Philipp Simon, Stephen Keable, Alexander Britz, Kensuke Tono, Kyung Sook Kim, Sang-Youn Park, Sang Jae Lee, Jaehyun Park, Roberto Alonso-Mori, Franklin D. Fuller, Alexander Batyuk, Aaron S. Brewster, Uwe Bergmann, Nicholas K. Sauter, Allen M. Orville, Vittal K. Yachandra, Junko Yano, John D. Lipscomb, Jan Kern, Martin Hogbom

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2020)

Article Optics

High-brightness self-seeded X-ray free-electron laser covering the 3.5 keV to 14.6 keV range

Inhyuk Nam, Chang-Ki Min, Bonggi Oh, Gyujin Kim, Donghyun Na, Young Jin Suh, Haeryong Yang, Myung Hoon Cho, Changbum Kim, Min-Jae Kim, Chi Hyun Shim, Jun Ho Ko, Hoon Heo, Jaehyun Park, Jangwoo Kim, Sehan Park, Gisu Park, Seonghan Kim, Sae Hwan Chun, HyoJung Hyun, Jae Hyuk Lee, Kyung Sook Kim, Intae Eom, Seungyu Rah, Deming Shu, Kwang-Je Kim, Sergey Terentyev, Vladimir Blank, Yuri Shvyd'ko, Sang Jae Lee, Heung-Sik Kang

Summary: The hard X-ray self-seeded X-ray free-electron laser at the Pohang Accelerator Laboratory offers high peak brightness and stability, providing superior data quality compared to SASE mode.

NATURE PHOTONICS (2021)

Article Biochemical Research Methods

Structural and functional studies of SAV1707 from Staphylococcus aureus elucidate its distinct metal-dependent activity and a crucial residue for catalysis

Dong Gyun Kim, Kyu Yeon Lee, Sang Jae Lee, Seung Ho Cheon, Yuri Choi, Hyung Ho Lee, Hee Chul Ahn, Bong Jin Lee

Summary: The metallo-beta-lactamase fold is a common metal-binding domain found in bacteria and archaea. Crystal structures of SAV1707, a metalloenzyme from Staphylococcus aureus, and its complex with cAMP were reported, revealing different metal selectivities for phosphodiesterase and endonuclease activities. Functional studies confirmed the role of residue Phe511 in substrate recognition.

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2021)

Article Genetics & Heredity

Structural Investigation of Self-Assembly and Target Binding of Anti-CRISPR AcrIIC2

Youngim Kim, Sang Jae Lee, Changkon Park, Jasung Koo, Euiyoung Bae, Bong-Jin Lee, Jeong-Yong Suh

Summary: AcrIIC2 inhibits the nuclease activity of type II-C Cas9, forming heterogeneous high-order oligomers driven by electrostatic interactions between charged residues. Upon binding with AcrIIC2, the BH peptide of Cas9 undergoes a coil-to-helix transition, revealing a unique folding-upon-binding mechanism for Acr recognition.

CRISPR JOURNAL (2021)

Article Biochemistry & Molecular Biology

Role of PemI in the Staphylococcus aureus PemIK toxin-antitoxin complex: PemI controls PemK by acting as a PemK loop mimic

Do-Hee Kim, Sung-Min Kang, Sung-Min Baek, Hye-Jin Yoon, Dong Man Jang, Hyoun Sook Kim, Sang Jae Lee, Bong-Jin Lee

Summary: Staphylococcus aureus, a pathogenic bacterium with global distribution, has been the focus of recent research on developing novel antibiotics based on its toxin-antitoxin systems. This study investigates the structure and function of the PemIK system in S. aureus, providing valuable information for the discovery and development of antibiotics that inhibit the direct binding between PemI and PemK.

NUCLEIC ACIDS RESEARCH (2022)

Article Multidisciplinary Sciences

Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I

Stephen M. Keable, Adrian Koelsch, Philipp S. Simon, Medhanjali Dasgupta, Ruchira Chatterjee, Senthil Kumar Subramanian, Rana Hussein, Mohamed Ibrahim, In-Sik Kim, Isabel Bogacz, Hiroki Makita, Cindy C. Pham, Franklin D. Fuller, Sheraz Gul, Daniel Paley, Louise Lassalle, Kyle D. Sutherlin, Asmit Bhowmick, Nigel W. Moriarty, Iris D. Young, Johannes P. Blaschke, Casper de Lichtenberg, Petko Chernev, Mun Hon Cheah, Sehan Park, Gisu Park, Jangwoo Kim, Sang Jae Lee, Jaehyun Park, Kensuke Tono, Shigeki Owada, Mark S. Hunter, Alexander Batyuk, Roland Oggenfuss, Mathias Sander, Serhane Zerdane, Dmitry Ozerov, Karol Nass, Henrik Lemke, Roman Mankowsky, Aaron S. Brewster, Johannes Messinger, Nicholas K. Sauter, Vittal K. Yachandra, Junko Yano, Athina Zouni, Jan Kern

Summary: The structure of cyanobacterial PS I at room temperature revealed an expansion of the protein complex compared to cryogenic structures. Conformational differences were observed between the two branches in the reaction center, which may provide insights into the preferential directionality of electron transfer.

SCIENTIFIC REPORTS (2021)

Article Biochemical Research Methods

Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adnesive proteins

Dong-Gyun Kim, Inwha Baek, Yeon Lee, Hyerry Kim, Jin Young Kim, Geul Bang, Sunghwan Kim, Hye Jin Yoon, Byung Woo Han, Se Won Suh, Hyoun Sook Kim

Summary: The initiation of host tissue infection by Staphylococcus aureus relies on a family of adhesive proteins containing SDR domains. This study elucidates a novel mechanism by which SdgB and SdgA carry out glycosyl-transfer processes and highlights the importance of their structures and activities in drug development against staphylococcal infections.

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2021)

Article Chemistry, Multidisciplinary

Radiation Damage of Polydimethylsiloxane and Polyimide by X-ray Free-Electron Laser

Keondo Lee, Donghyeon Lee, Sangwon Baek, Jihan Kim, Jaehyun Park, Sang Jae Lee, Sehan Park, Jangwoo Kim, Jong-Lam Lee, Wan Kyun Chung, Yunje Cho, Ki Hyun Nam

Summary: This study investigated the radiation damage caused by an XFEL to PDMS and PI materials, commonly used in sample delivery devices. The results showed different structural damages in PDMS and PI films, providing insights for developing applications of these materials in XFEL studies.

APPLIED SCIENCES-BASEL (2022)

Article Biochemistry & Molecular Biology

Structure-based drug discovery of a corticotropin-releasing hormone receptor 1 antagonist using an X-ray free-electron laser

Hoyoung Kim, Taehyun Lim, Go Eun Ha, Jee-Young Lee, Jun-Woo Kim, Nienping Chang, Si Hyun Kim, Ki Hun Kim, Jaeick Lee, Yongju Cho, Byeong Wook Kim, Alva Abrahamsson, Sung Hwan Kim, Hyo-Ji Kim, Sehan Park, Sang Jae Lee, Jaehyun Park, Eunji Cheong, B. Moon Kim, Hyun-Soo Cho

Summary: This study utilizes X-ray free electron laser technology to determine the structural characteristics of the corticotropin-releasing hormone receptor 1 protein complexes and develops potential antidepressant antagonist compounds.

EXPERIMENTAL AND MOLECULAR MEDICINE (2023)

No Data Available