期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 187, 期 2, 页码 174-186出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2014.06.001
关键词
Protein crystallography; Nuclear magnetic resonance; N-terminal domain; delta-Subunit; RNA polymerase
资金
- Czech Science Foundation [GA13-16842S]
- project 'CEITEC - Central European Institute of Technology' from the European Regional Development Fund [CZ.1.05/1.1.00/02.0068]
- project, Employment of Newly Graduated Doctors of Science for Scientific Excellence from European Social Fund [CZ.1.07/2.3.00/30.0009]
- state budget of the Czech Republic
The crystal structure of the N-terminal domain of the RNA polymerase delta subunit (N delta) from Bacillus subtilis solved at a resolution of 2.0 angstrom is compared with the NMR structure determined previously. The molecule crystallizes in the space group C222(1) with a dimer in the asymmetric unit. Importantly, the X-ray structure exhibits significant differences from the lowest energy NMR structure. In addition to the overall structure differences, structurally important beta sheets found in the NMR structure are not present in the crystal structure. We systematically investigated the cause of the discrepancies between the NMR and X-ray structures of NB, addressing the pH dependence, presence of metal ions, and crystal packing forces. We convincingly showed that the crystal packing forces, together with the presence of Ni2+ ions, are the main reason for such a difference. In summary, the study illustrates that the two structural approaches may give unequal results, which need to be interpreted with care to obtain reliable structural information in terms of biological relevance. (C) 2014 Elsevier Inc. All rights reserved.
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