TIME-RESOLVED X-RAY CRYSTALLOGRAPHIC STUDY OF THE CONFORMATIONAL CHANGE IN HA-RAS P21 PROTEIN ON GTP HYDROLYSIS

被引：468

作者：

SCHLICHTING, I

ALMO, SC

RAPP, G

WILSON, K

PETRATOS, K

LENTFER, A

WITTINGHOFER, A

KABSCH, W

PAI, EF

PETSKO, GA

GOODY, RS

机构：

[1] MAX PLANCK INST MED RES,BIOPHYS ABT,W-6900 HEIDELBERG 1,GERMANY

[2] MIT,DEPT CHEM,CAMBRIDGE,MA 02139

[3] DESY,EUROPEAN MOLEC BIOL LAB OUTSTN,W-2000 HAMBURG,GERMANY

来源：

NATURE | 1990年 / 345卷 / 6273期

关键词：

D O I：

10.1038/345309a0

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：

Crystals of Ha-Ras p21 with caged GTP at the active site have been used to investigate the conformational changes of p21 on GTP hydrolysis. The structure of the short-lived p21-GTP complex was determined by Laue diffraction methods. After GTP hydrolysis, substantial structural changes occur in the parts of the molecule implicated in the interaction with GTPase-activating protein. The trigger for this process seems to be a change in coordination of the active-site Mg2+ion as a result of loss of the γ-phosphate of GTP. © 1990 Nature Publishing Group.

引用

页码：309 / 315

页数：7

共 35 条

[1] GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN (GAP) INTERACTS WITH THE P21-RAS EFFECTOR BINDING DOMAIN [J].