2ot2
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | Escherichia coli HypC plays an important role in the maturation process of | + | 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== | ==About this Structure== | ||
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[[Category: chaperone]] | [[Category: chaperone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:22:15 2008'' |
Revision as of 16:22, 21 February 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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