1G2I

CRYSTAL STRUCTURE OF A NOVEL INTRACELLULAR PROTEASE FROM PYROCOCCUS HORIKOSHII AT 2 A RESOLUTION

Summary for 1G2I

• Entry DOI: 10.2210/pdb1g2i/pdb
• Descriptor: PROTEASE I, SULFATE ION (3 entities in total)
• Functional Keywords: intracellular protease, atp-independent intracellular protease, protease, catalytical triad, pfpi, cysteine protease, nucleophile elbow, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, hydrolase
• Biological source: Pyrococcus horikoshii
• Cellular location: Cytoplasm : O59413
• Total number of polymer chains: 3
• Total formula weight: 56610.06

Authors

Du, X.,Choi, I.-G.,Kim, R.,Jancarik, J.,Kim, S.-H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 2000-10-19, release date: 2000-11-08, Last modification date: 2024-10-16)

Primary citation

Du, X.,Choi, I.G.,Kim, R.,Wang, W.,Jancarik, J.,Yokota, H.,Kim, S.-H.
Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.
Proc.Natl.Acad.Sci.USA, 97:14079-14084, 2000

PubMed Abstract: 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.

PubMed: 11114201
DOI: 10.1073/pnas.260503597

Experimental method

X-RAY DIFFRACTION (2 Å)