期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 425, 期 14, 页码 2436-2449出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2013.03.035
关键词
phage morphogenesis; tail assembly; x-ray crystal structure; protein evolution; oligomerization mechanisms
资金
- Canadian Institutes of Health Research [MOP-62796, MOP-77680]
- Natural Sciences and Engineering Research Council of Canada CGS-D scholarship
- Ontario Research and Development Challenge Fund [99-SEP-0512]
- Canada Research Program
- U.S. Department of Energy, Office of Basic Energy Sciences [W-31-109-Eng-38]
- Center for Advanced Radiation Sources at the University of Chicago
Tail assembly chaperones (TACs) are a family of proteins likely required for the morphogenesis of all long-tailed phages. In this study, we determined the crystal structure of gp13, the TAC of phage HK97. This structure is similar to that of the TAC from the Lactococcus phage p2 and two unannotated structures of likely TACs encoded in prophage-derived regions of Bacillus subtilis and Bacillus stearothermophilus. Despite the high sequence divergence of these proteins, gp13 forms a ring structure with similar dimensions to the spirals observed in the crystal lattices of these other proteins. Remarkably, these-similar quaternary structures are formed through very different interprotomer interactions. We present functional data supporting the biological relevance of these spiral structures and propose that spiral formation has been the primary requirement for these proteins during evolution. This study presents an unusual example of diverged protein sequences and oligomerization mechanisms in the presence of conserved quaternary structure. Crown Copyright (C) 2013 Published by Elsevier Ltd. All rights reserved.
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