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2ot2
From Proteopedia
Revision as of 19:50, 30 September 2014 by OCA (Talk | contribs)
2ot2 is a 1 chain structure with sequence from Escherichia coli k-12. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Wang L, Xia B, Jin C. Solution structure of Escherichia coli HypC. Biochem Biophys Res Commun. 2007 Sep 28;361(3):665-9. Epub 2007 Jul 26. PMID:17669368 doi:10.1016/j.bbrc.2007.07.094
