1g2i
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(New page: 200px<br /><applet load="1g2i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g2i, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 13:31, 20 November 2007
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CRYSTAL STRUCTURE OF A NOVEL INTRACELLULAR PROTEASE FROM PYROCOCCUS HORIKOSHII AT 2 A RESOLUTION
Overview
The intracellular protease from Pyrococcus horikoshii (PH1704) and PfpI, from Pyrococcus furiosus are members of a class of intracellular proteases, that have no sequence homology to any other known protease family. We, report the crystal structure of PH1704 at 2.0-A resolution. The protease, is tentatively identified as a cysteine protease based on the presence of, cysteine (residue 100) in a nucleophile elbow motif. In the crystal, PH1704 forms a hexameric ring structure, and the active sites are formed, at the interfaces between three pairs of monomers.
About this Structure
1G2I is a Single protein structure of sequence from Pyrococcus horikoshii with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution., Du X, Choi IG, Kim R, Wang W, Jancarik J, Yokota H, Kim SH, Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14079-84. PMID:11114201
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Categories: Pyrococcus horikoshii | Single protein | BSGC, Berkeley.Structural.Genomics.Center. | Choi, I-G. | Du, X. | Jancarik, J. | Kim, R. | Kim, S.H. | SO4 | Atp-independent intracellular protease | Berkeley structural genomics center | Bsgc structure funded by nih | Catalytical triad | Cysteine protease | Intracellular protease | Nucleophile elbow | Pfpi | Protease | Protein structure initiative | Psi | Structural genomics
