Structural highlights
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 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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Du X, Choi IG, Kim R, Wang W, Jancarik J, Yokota H, Kim SH. Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution. Proc Natl Acad Sci U S A. 2000 Dec 19;97(26):14079-84. PMID:11114201 doi:10.1073/pnas.260503597
