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Elucidating the GTP Hydrolysis Mechanism in FeoB – a Hydrophobic Amino Acid Substituted GTPase.

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Relation http://ir.cftri.com/13347/
http://dx.doi.org/10.1021/acscatal.6b03365
 
Title Elucidating the GTP Hydrolysis Mechanism in FeoB
– a Hydrophobic Amino Acid Substituted GTPase.
 
Creator Neha, Vithani
Sahil, Batra
Balaji, Prakash
Nisanth, N. Nair
 
Subject 07 Enzyme Biochemistry
 
Description Employing hybrid quantum mechanics/molecular dynamics (QM/MM) molecular dynamics simulations and experimental mutational studies, we investigate the GTP hydrolysis mechanism in a hydrophobic amino-acid substituted (HAS)-GTPase, FeoB. We identify glutamates, Glu66 and Glu67, that are acting as bases and find that proton transfer occurs from the attacking water to either of the glutamates through a water chain. However, GTP hydrolysis is not abolished, despite mutating these glutamates; instead, an alternative substrate-assisted hydrolysis becomes active with the same rate. Thus, mutational studies would misinterpret the role of glutamates. We trace the origin of the alternative mechanism to a structural feature conserved across all HAS-GTPases, distinct from the Ras-like GTPases.
 
Date 2017
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/13347/1/ACS%20Catal.%2C%202017%2C%207%20%281%29%2C%20pp%20902%E2%80%93906.pdf
Neha, Vithani and Sahil, Batra and Balaji, Prakash and Nisanth, N. Nair (2017) Elucidating the GTP Hydrolysis Mechanism in FeoB – a Hydrophobic Amino Acid Substituted GTPase. ACS Catalysis, 7 (1). pp. 902-906.