1g2i
CRYSTAL STRUCTURE OF A NOVEL INTRACELLULAR PROTEASE FROM PYROCOCCUS HORIKOSHII AT 2 A RESOLUTION
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| , resolution 2.00Å | |||||||
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| Ligands: | |||||||
| Gene: | PH1704 (Pyrococcus horikoshii) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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 StructureAbout this Structure
1G2I is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
ReferenceReference
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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