Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Ilme Schlichting; Steven C. Almo; Gert Rapp; Keith Wilson; Kyriakos Petratos; Arno Lentfer; Alfred Wittinghofer; Wolfgang Kabsch; Emil F. Pai; Gregory A. Petsko; Roger S. Goody

doi:10.1038/345309a0

Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Ilme Schlichting
, Steven C. Almo
, Gert Rapp
, Keith Wilson
, Kyriakos Petratos
, Arno Lentfer
, Alfred Wittinghofer
, Wolfgang Kabsch
, Emil F. Pai
, Gregory A. Petsko
, Roger S. Goody

Research output: Contribution to journal › Article › peer-review

465 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	309-315
Number of pages	7
Journal	Nature
Volume	345
Issue number	6273
DOIs	https://doi.org/10.1038/345309a0
State	Published - 1990
Externally published	Yes

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@article{90ad4c9e16fe4ccabdbf555107e7d29f,

title = "Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis",

abstract = "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.",

author = "Ilme Schlichting and Almo, \{Steven C.\} and Gert Rapp and Keith Wilson and Kyriakos Petratos and Arno Lentfer and Alfred Wittinghofer and Wolfgang Kabsch and Pai, \{Emil F.\} and Petsko, \{Gregory A.\} and Goody, \{Roger S.\}",

year = "1990",

doi = "10.1038/345309a0",

language = "English (US)",

volume = "345",

pages = "309--315",

journal = "Nature",

issn = "0028-0836",

publisher = "Nature Research",

number = "6273",

}

TY - JOUR

T1 - Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

AU - Schlichting, Ilme

AU - Almo, Steven C.

AU - Rapp, Gert

AU - Wilson, Keith

AU - Petratos, Kyriakos

AU - Lentfer, Arno

AU - Wittinghofer, Alfred

AU - Kabsch, Wolfgang

AU - Pai, Emil F.

AU - Petsko, Gregory A.

AU - Goody, Roger S.

PY - 1990

Y1 - 1990

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0025275582

UR - https://www.scopus.com/pages/publications/0025275582#tab=citedBy

U2 - 10.1038/345309a0

DO - 10.1038/345309a0

M3 - Article

C2 - 2111463

AN - SCOPUS:0025275582

SN - 0028-0836

VL - 345

SP - 309

EP - 315

JO - Nature

JF - Nature

IS - 6273

ER -

Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Abstract

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