2E85
Crystal Structure of the Hydrogenase 3 Maturation protease
Summary for 2E85
Entry DOI | 10.2210/pdb2e85/pdb |
Descriptor | Hydrogenase 3 maturation protease, CALCIUM ION (3 entities in total) |
Functional Keywords | hydrogenase, maturation, protease, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 34767.67 |
Authors | Tanaka, T.,Kumarevel, T.S.,Shinkai, A.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2007-01-18, release date: 2008-01-22, Last modification date: 2024-05-29) |
Primary citation | Kumarevel, T.,Tanaka, T.,Bessho, Y.,Shinkai, A.,Yokoyama, S. Crystal structure of hydrogenase maturating endopeptidase HycI from Escherichia coli Biochem.Biophys.Res.Commun., 389:310-314, 2009 Cited by PubMed Abstract: 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. PubMed: 19720045DOI: 10.1016/j.bbrc.2009.08.135 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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