Refinement of the arginine kinase transition-state analogue complex at 1.2 Å resolution: Mechanistic insights

Mohammad S. Yousef; Felcy Fabiola; James L. Gattis; Thayumanasamy Somasundaram; Michael S. Chapman

doi:10.1107/S0907444902014683

Refinement of the arginine kinase transition-state analogue complex at 1.2 Å resolution: Mechanistic insights

Mohammad S. Yousef, Felcy Fabiola, James L. Gattis, Thayumanasamy Somasundaram, Michael S. Chapman

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

63 Scopus citations

Abstract

The transition-state complex of this 42 kDa homologue of creatine kinase has been refined at 1.2 Å resolution. It indicates that precise positioning of substrates and restriction of the active-site motion are important components in catalysis.

Original language	English (US)
Pages (from-to)	2009-2017
Number of pages	9
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	58
Issue number	12
DOIs	https://doi.org/10.1107/S0907444902014683
State	Published - Dec 1 2002
Externally published	Yes

ASJC Scopus subject areas

Structural Biology

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title = "Refinement of the arginine kinase transition-state analogue complex at 1.2 {\AA} resolution: Mechanistic insights",

abstract = "The transition-state complex of this 42 kDa homologue of creatine kinase has been refined at 1.2 {\AA} resolution. It indicates that precise positioning of substrates and restriction of the active-site motion are important components in catalysis.",

author = "Yousef, {Mohammad S.} and Felcy Fabiola and Gattis, {James L.} and Thayumanasamy Somasundaram and Chapman, {Michael S.}",

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AU - Yousef, Mohammad S.

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AU - Somasundaram, Thayumanasamy

AU - Chapman, Michael S.

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Refinement of the arginine kinase transition-state analogue complex at 1.2 Å resolution: Mechanistic insights

Abstract

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