期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 332, 期 4, 页码 767-776出版社
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD
DOI: 10.1016/S0022-2836(03)00918-5
关键词
phosphotransferase system; carbon catabolite repression; Crh; X-ray structure; domain swapped dimer
The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8 Angstrom resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity. (C) 2003 Elsevier Ltd. All rights reserved.
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