3gar: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
3GAR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ | 3GAR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Phosphoribosylglycinamide_formyltransferase Phosphoribosylglycinamide formyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.2 2.1.2.2]]. Structure known Active Site: E70. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3GAR OCA]]. | ||
==Reference== | ==Reference== | ||
A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A., Su Y, Yamashita MM, Greasley SE, Mullen CA, Shim JH, Jennings PA, Benkovic SJ, Wilson IA, J Mol Biol. 1998 Aug 21;281(3):485-99. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9698564 9698564] | A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A., Su Y, Yamashita MM, Greasley SE, Mullen CA, Shim JH, Jennings PA, Benkovic SJ, Wilson IA, J Mol Biol. 1998 Aug 21;281(3):485-99. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9698564 9698564] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphoribosylglycinamide formyltransferase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Benkovic, S.J.]] | [[Category: Benkovic, S.J.]] | ||
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[[Category: purine biosynthesis]] | [[Category: purine biosynthesis]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:30:01 2007'' | ||
Revision as of 11:25, 30 October 2007
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A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
OverviewOverview
A mutation in the dimer interface of Escherichia coli glycinamide, ribonucleotide transformylase (GarTfase) disrupts the observed, pH-dependent association of the wild-type enzyme, but has no observable, effect on the enzyme activity. Here, we assess whether a pH effect on the, enzyme's conformation is sufficient by itself to explain the pH-dependence, of the GarTfase reaction. A pH-dependent conformational change is observed, between two high-resolution crystal structures of the Glu70Ala mutant, GarTfase at pH 3.5 (1.8 A) and 7.5 (1.9 A). Residues 110 to 131 in, GarTfase undergo a transformation from a disordered loop at pH 3.5, where, the enzyme is inactive, to an ordered loop-helix structure at pH 7.5, where the enzyme is active. The ordering of this flexible loop-helix has a, direct ... [(full description)]
About this StructureAbout this Structure
3GAR is a [Single protein] structure of sequence from [Escherichia coli] with PO4 as [ligand]. Active as [Phosphoribosylglycinamide formyltransferase], with EC number [2.1.2.2]. Structure known Active Site: E70. Full crystallographic information is available from [OCA].
ReferenceReference
A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A., Su Y, Yamashita MM, Greasley SE, Mullen CA, Shim JH, Jennings PA, Benkovic SJ, Wilson IA, J Mol Biol. 1998 Aug 21;281(3):485-99. PMID:9698564
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OCA- Pages with broken file links
- Escherichia coli
- Phosphoribosylglycinamide formyltransferase
- Single protein
- Benkovic, S.J.
- Greasley, S.E.
- Jennings, P.A.
- Mullen, C.A.
- Shim, J.H.
- Su, Y.
- Wilson, I.A.
- Yamashita, M.M.
- PO4
- Anti-cancer agents
- Enzyme mechanism
- Folate cofactors
- Loop flexibility
- Monomer-dimer association
- Purine biosynthesis