4pga
From Proteopedia
(New page: 200px<br /> <applet load="4pga" size="450" color="white" frame="true" align="right" spinBox="true" caption="4pga, resolution 1.7Å" /> '''GLUTAMINASE-ASPARAGI...) |
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==About this Structure== | ==About this Structure== | ||
| - | 4PGA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_sp._7a Pseudomonas sp. 7a]] with SO4 and NH4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.38 3.5.1.38]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4PGA OCA]]. | + | 4PGA is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pseudomonas_sp._7a Pseudomonas sp. 7a]] with SO4 and NH4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Glutamin-(asparagin-)ase Glutamin-(asparagin-)ase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.38 3.5.1.38]]. Structure known Active Sites: AS1 and AS2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4PGA OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9020792 9020792] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9020792 9020792] | ||
| + | [[Category: Glutamin-(asparagin-)ase]] | ||
[[Category: Pseudomonas sp. 7a]] | [[Category: Pseudomonas sp. 7a]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: bacterial amidohydrolase]] | [[Category: bacterial amidohydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:53:26 2007'' |
Revision as of 08:48, 30 October 2007
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GLUTAMINASE-ASPARAGINASE FROM PSEUDOMONAS 7A
Overview
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 ... [(full description)]
About this Structure
4PGA is a [Single protein] structure of sequence from [Pseudomonas sp. 7a] with SO4 and NH4 as [ligands]. Active as [Glutamin-(asparagin-)ase], with EC number [3.5.1.38]. Structure known Active Sites: AS1 and AS2. 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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