1bgv

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{{STRUCTURE_1bgv| PDB=1bgv | SCENE= }}
{{STRUCTURE_1bgv| PDB=1bgv | SCENE= }}
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'''GLUTAMATE DEHYDROGENASE'''
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===GLUTAMATE DEHYDROGENASE===
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==Overview==
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We have solved the structure of the binary complex of the glutamate dehydrogenase from Clostridium symbiosum with glutamate to 1.9 A resolution. In this complex, the glutamate side-chain lies in a pocket on the enzyme surface and a key determinant of the enzymic specificity is an interaction of the substrate gamma-carboxyl group with the amino group of Lys89. In the apo-enzyme, Lys113 from the catalytic domain forms an important hydrogen bond to Asn373, in the NAD(+)-binding domain. On glutamate binding, the side-chain of this lysine undergoes a significant movement in order to optimize its hydrogen bonding to the alpha-carboxyl group of the substrate. Despite this shift, the interaction between Lys113 and Asn373 is maintained by a large-scale conformational change that closes the cleft between the two domains. Modelling studies indicate that in this "closed" conformation the C-4 of the nicotinamide ring and the alpha-carbon atom of the amino acid substrate are poised for efficient hydride transfer. Examination of the structure has led to a proposal for the catalytic activity of the enzyme, which involves Asp165 as a general base, and an enzyme-bound water molecule, hydrogen-bonded to an uncharged lysine residue, Lys125, as an attacking nucleophile in the reaction.
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(as it appears on PubMed at http://www.pubmed.gov), where 8263917 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8263917}}
==About this Structure==
==About this Structure==
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[[Category: Stillman, T J.]]
[[Category: Stillman, T J.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:29:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:08:19 2008''

Revision as of 16:08, 30 June 2008

Image:1bgv.png

Template:STRUCTURE 1bgv

GLUTAMATE DEHYDROGENASE

Template:ABSTRACT PUBMED 8263917

About this Structure

1BGV is a Single protein structure of sequence from Clostridium symbiosum. Full crystallographic information is available from OCA.

Reference

Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis., Stillman TJ, Baker PJ, Britton KL, Rice DW, J Mol Biol. 1993 Dec 20;234(4):1131-9. PMID:8263917

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