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

被引：92

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

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2000年 / 97卷 / 26期

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.

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页码：14079 / 14084

页数：6

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