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4pga

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{{STRUCTURE_4pga| PDB=4pga | SCENE= }}
{{STRUCTURE_4pga| PDB=4pga | SCENE= }}
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'''GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A'''
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===GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A===
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==Overview==
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Pseudomonas 7A glutaminase-asparaginase (PGA) catalyzes the hydrolysis of D- and L-isomers of glutamine and asparagine. X-ray quality type-1 crystals of PGA have been obtained from 2.0 M ammonium sulfate. The space group is C222(1) with unit-cell dimensions a = 78.62, b = 135.80, and c = 137.88 A. The tetrameric molecule is located on a crystallographic 2-fold axis, and two subunits form the asymmetric portion of the unit cell. The structure was solved by the molecular replacement method and refined at 1.7 A resolution to an R = 19.9% with a good geometry of the model, G = 0.05. The resultant electron density maps enabled us to resolve individual constituent atoms of most residues and introduce minor revisions to the amino acid sequence. The catalytic loop, Thr20-Gly40, is in the closed conformation with excellent electron density in both subunits. A sulfate ion and an ammonium ion are bound in the substrate binding site and interect with the loop. This interaction appears to be responsible for the observed closed conformation. New arguments supporting Thr20 as the catalytic nucleophile in the asparaginase activity are proposed.
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{{ABSTRACT_PUBMED_9020792}}
==About this Structure==
==About this Structure==
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[[Category: Roberts, J.]]
[[Category: Roberts, J.]]
[[Category: Bacterial amidohydrolase]]
[[Category: Bacterial amidohydrolase]]
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Revision as of 10:47, 3 July 2008

Image:4pga.png

Template:STRUCTURE 4pga

GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A

Template:ABSTRACT PUBMED 9020792

About this Structure

4PGA is a Single protein structure of sequence from Pseudomonas sp. 7a. Full crystallographic information is available from OCA.

Reference

Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution., Jakob CG, Lewinski K, LaCount MW, Roberts J, Lebioda L, Biochemistry. 1997 Jan 28;36(4):923-31. PMID:9020792

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