Proteins: Structure, Function and Genetics, volume 83, issue 11, pages 2091-2099

Why does mutation of Gln61 in Ras by the nitro analog NGln maintain activity of Ras-GAP in hydrolysis of guanosine triphosphate?

Khrenova Maria G. ¹

Grigorenko Bella ^{1, 2}

Mironov Vladimir ¹

Nemukhin Alexander ^{1, 2}

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Chemistry Department; M.V. Lomonosov Moscow State University; 1-3 Leninskie Gory Moscow 119991 Russia |

N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences; 4 Kosygin Street Moscow 119334 Russia |

Publication type: Journal Article

Publication date: 2015-09-29

Wiley

Journal: Proteins: Structure, Function and Genetics

Quartile SCImago

Quartile WOS

Impact factor: 2.9

ISSN: 08873585, 10970134

DOI: 10.1002/prot.24927

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Biochemistry

Molecular Biology

Structural Biology

Abstract

Interpretation of the experiments showing that the Ras‐GAP protein complex maintains activity in guanosine triphosphate (GTP) hydrolysis upon replacement of Glu61 in Ras with its unnatural nitro analog, NGln, is an important issue for understanding details of chemical transformations at the enzyme active site. By using molecular modeling we demonstrate that both glutamine and its nitro analog in the aci‐nitro form participate in the reaction of GTP hydrolysis at the stages of proton transfer and formation of inorganic phosphate. The computed structures and the energy profiles for the complete pathway from the enzyme‐substrate to enzyme‐product complexes for the wild‐type and mutated Ras suggest that the reaction mechanism is not affected by this mutation. Proteins 2015; 83:2091–2099. © 2015 Wiley Periodicals, Inc.

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Citations by journals

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Journal of Physical Chemistry B	Journal of Physical Chemistry B, 3, 33.33% Journal of Physical Chemistry B 3 publications, 33.33%
Organic and Biomolecular Chemistry	Organic and Biomolecular Chemistry, 1, 11.11% Organic and Biomolecular Chemistry 1 publication, 11.11%
Physical Chemistry Chemical Physics	Physical Chemistry Chemical Physics, 1, 11.11% Physical Chemistry Chemical Physics 1 publication, 11.11%
Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy	Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy, 1, 11.11% Spectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopy 1 publication, 11.11%
Topics in Current Chemistry	Topics in Current Chemistry, 1, 11.11% Topics in Current Chemistry 1 publication, 11.11%
Biophysical Chemistry	Biophysical Chemistry, 1, 11.11% Biophysical Chemistry 1 publication, 11.11%
Proteins: Structure, Function and Genetics	Proteins: Structure, Function and Genetics, 1, 11.11% Proteins: Structure, Function and Genetics 1 publication, 11.11%
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Citations by publishers

	1 2 3
American Chemical Society (ACS)	American Chemical Society (ACS), 3, 33.33% American Chemical Society (ACS) 3 publications, 33.33%
Royal Society of Chemistry (RSC)	Royal Society of Chemistry (RSC), 2, 22.22% Royal Society of Chemistry (RSC) 2 publications, 22.22%
Elsevier	Elsevier, 2, 22.22% Elsevier 2 publications, 22.22%
Springer Nature	Springer Nature, 1, 11.11% Springer Nature 1 publication, 11.11%
Wiley	Wiley, 1, 11.11% Wiley 1 publication, 11.11%
	1 2 3

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Khrenova M. G. et al. Why does mutation of Gln61 in Ras by the nitro analog NGln maintain activity of Ras-GAP in hydrolysis of guanosine triphosphate? // Proteins: Structure, Function and Genetics. 2015. Vol. 83. No. 11. pp. 2091-2099.

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Khrenova M. G., Grigorenko B., Mironov V., Nemukhin A. Why does mutation of Gln61 in Ras by the nitro analog NGln maintain activity of Ras-GAP in hydrolysis of guanosine triphosphate? // Proteins: Structure, Function and Genetics. 2015. Vol. 83. No. 11. pp. 2091-2099.

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