期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 3, 页码 E202-E211出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1208134110
关键词
Staphylococci; X-ray crystallography; zinc; self-assembly; G5 domain
资金
- National Institutes of Health [R01 GM094363]
- Midwest Center for Emerging Infectious Diseases at the University of Cincinnati
- State of Ohio Eminent Scholar program
- National Center for Research Resources at the National Institutes of Health [RR-15301]
- US Department of Energy, Office of Basic Energy Sciences [W-31-109-ENG-38]
Staphylococcal bacteria, including Staphylococcus epidermidis and Staphylococcus aureus, cause chronic biofilm-related infections. The homologous proteins Aap and SasG mediate biofilm formation in S. epidermidis and S. aureus, respectively. The self-association of these proteins in the presence of Zn2+ leads to the formation of extensive adhesive contacts between cells. This study reports the crystal structure of a Zn2+-bound construct from the self-associating region of Aap. Several unusual structural features include elongated beta-sheets that are solvent-exposed on both faces and the lack of a canonical hydrophobic core. Zn2+-dependent dimers are observed in three distinct crystal forms, formed via pleomorphic coordination of Zn2+ in trans across the dimer interface. These structures illustrate how a long, flexible surface protein is able to form tight intercellular adhesion sites under adverse environmental conditions.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据