Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution

被引:91
作者
Du, XL
Choi, IG
Kim, R
Wang, WR
Jancarik, J
Yokota, H
Kim, SH [1 ]
机构
[1] Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Lawrence Berkeley Lab, Dept Biol Struct, Phys Biosci Div, Berkeley, CA 94720 USA
关键词
D O I
10.1073/pnas.260503597
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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-Angstrom 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.
引用
收藏
页码:14079 / 14084
页数:6
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