1e7y: Difference between revisions

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[[Image:1e7y.jpg|left|200px]]
{{Seed}}
[[Image:1e7y.png|left|200px]]


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{{STRUCTURE_1e7y|  PDB=1e7y  |  SCENE=  }}  
{{STRUCTURE_1e7y|  PDB=1e7y  |  SCENE=  }}  


'''ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES COMPLEXED WITH SUBSTRATE AND NADPH'''
===ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES COMPLEXED WITH SUBSTRATE AND NADPH===




==Overview==
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The role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides has been investigated by a structural and functional characterization of the D177N mutant enzyme. Its three-dimensional structure has been determined by X-ray cryocrystallography in the presence of NAD(+) and in the presence of glucose 6-phosphate plus NADPH. The structure of a glucose 6-phosphate complex of a mutant (Q365C) with normal enzyme activity has also been determined and substrate binding compared. To understand the effect of Asp-177 on the ionization properties of the catalytic base His-240, the pH dependence of kinetic parameters has been determined for the D177N mutant and compared to that of the wild-type enzyme. The structures give details of glucose 6-phosphate binding and show that replacement of the Asp-177 of the catalytic dyad with asparagine does not affect the overall structure of glucose 6-phosphate dehydrogenase. Additionally, the evidence suggests that the productive tautomer of His-240 in the D177N mutant enzyme is stabilized by a hydrogen bond with Asn-177; hence, the mutation does not affect tautomer stabilization. We conclude, therefore, that the absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8. Structural analysis suggests that the pH dependence of the kinetic parameters of D177N glucose 6-phosphate dehydrogenase results from an ionized water molecule replacing the missing negative charge of the mutated Asp-177 at high pH. Glucose 6-phosphate binding orders and orients His-178 in the D177N-glucose 6-phosphate-NADPH ternary complex and appears to be necessary to form this water-binding site.
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{{ABSTRACT_PUBMED_11106478}}


==About this Structure==
==About this Structure==
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[[Category: Gover, S.]]
[[Category: Gover, S.]]
[[Category: Glucose metabolism]]
[[Category: Glucose metabolism]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:46:30 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:17:46 2008''

Revision as of 21:17, 30 June 2008

File:1e7y.png

Template:STRUCTURE 1e7y

ACTIVE SITE MUTANT (D177->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES COMPLEXED WITH SUBSTRATE AND NADPH

Template:ABSTRACT PUBMED 11106478

About this Structure

1E7Y is a Single protein structure of sequence from Leuconostoc mesenteroides. Full crystallographic information is available from OCA.

Reference

An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme., Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR, Biochemistry. 2000 Dec 12;39(49):15002-11. PMID:11106478

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