Structural highlights
Function
[HYCI_ECOLI] Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The maturation of [NiFe]-hydrogenases is a catalyzed process involving the activities of at least seven proteins. The last step consists of the endoproteolytic cleavage of the precursor of the large subunit, after the [NiFe]-metal center has been assembled. The HycI endopeptidase is involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3 from Escherichia coli. Although HycI has been well characterized biochemically, the crystallization of the protein has been quite challenging. Here, we present the crystal structure of HycI at 1.70 A resolution. The crystal structure resembles the recently reported solution structure (NMR) of the same protein and the holo-HyPD structure of the same family, but a significant conformational change is observed at the L5 loop, as compared with the solution structures of HycI and HyPD. In our crystal structure, three specific metal binding sites (Ca1-3) were identified and these metal ions are possibly involved in the C-terminal cleavage of HycE.
Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli.,Kumarevel T, Tanaka T, Bessho Y, Shinkai A, Yokoyama S Biochem Biophys Res Commun. 2009 Nov 13;389(2):310-4. Epub 2009 Aug 29. PMID:19720045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kumarevel T, Tanaka T, Bessho Y, Shinkai A, Yokoyama S. Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli. Biochem Biophys Res Commun. 2009 Nov 13;389(2):310-4. Epub 2009 Aug 29. PMID:19720045 doi:10.1016/j.bbrc.2009.08.135
