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1e77

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[[Image:1e77.gif|left|200px]]
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{{Seed}}
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[[Image:1e77.png|left|200px]]
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{{STRUCTURE_1e77| PDB=1e77 | SCENE= }}
{{STRUCTURE_1e77| PDB=1e77 | SCENE= }}
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'''COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE'''
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===COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 11106478 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11106478}}
==About this Structure==
==About this Structure==
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[[Category: Vandeputte-Rutten, L.]]
[[Category: Vandeputte-Rutten, L.]]
[[Category: Glucose metabolism]]
[[Category: Glucose metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:44:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:16:02 2008''

Revision as of 21:16, 30 June 2008

Image:1e77.png

Template:STRUCTURE 1e77

COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE

Template:ABSTRACT PUBMED 11106478

About this Structure

1E77 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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