2ot2
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(New page: 200px<br /><applet load="2ot2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ot2" /> '''Solution Structure of HypC'''<br /> ==Overv...)
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Revision as of 11:46, 23 January 2008
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Solution Structure of HypC
Overview
Escherichia coli HypC plays an important role in the maturation process of, the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as, an iron transfer as well as a chaperone protein during the maturation, process of pre-HycE, and interacts with both HypD and HycE. The N-terminal, cysteine residue of HypC plays a key role in the protein-protein, interactions. Here, we present the three-dimensional structure of E. coli, HypC, the first solution structure of HupF/HypC family. Our result, demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel, with two C-terminal helixes. Sequence alignment and structural comparison, reveal that the hydrophobic region on the surface of E. coli HypC, as well, as the highly flexible C-terminal helixes, may involve in the interactions, of E. coli HypC with other proteins.
About this Structure
2OT2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of Escherichia coli HypC., Wang L, Xia B, Jin C, Biochem Biophys Res Commun. 2007 Sep 28;361(3):665-9. Epub 2007 Jul 26. PMID:17669368
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