1e58: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
1E58 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 SO4 and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. The following page contains interesting information on the relation of 1E58 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [[http://en.wikipedia.org/wiki/ | 1E58 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 SO4 and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. The following page contains interesting information on the relation of 1E58 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [[http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1]]. Structure known Active Site: HIS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E58 OCA]]. | ||
==Reference== | ==Reference== | ||
High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase., Bond CS, White MF, Hunter WN, J Biol Chem. 2001 Feb 2;276(5):3247-53. Epub 2000 Oct 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11038361 11038361] | High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase., Bond CS, White MF, Hunter WN, J Biol Chem. 2001 Feb 2;276(5):3247-53. Epub 2000 Oct 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11038361 11038361] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphoglycerate mutase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: The Glycolytic Enzymes]] | [[Category: The Glycolytic Enzymes]] | ||
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[[Category: phosphohistidine]] | [[Category: phosphohistidine]] | ||
''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 10:51:11 2007'' | ||
Revision as of 11:46, 30 October 2007
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E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE
OverviewOverview
The active conformation of the dimeric cofactor-dependent phosphoglycerate, mutase (dPGM) from Escherichia coli has been elucidated by, crystallographic methods to a resolution of 1.25 A (R-factor 0.121; R-free, 0.168). The active site residue His(10), central in the catalytic, mechanism of dPGM, is present as a phosphohistidine with occupancy of, 0.28. The structural changes on histidine phosphorylation highlight, various features that are significant in the catalytic mechanism. The, C-terminal 10-residue tail, which is not observed in previous dPGM, structures, is well ordered and interacts with residues implicated in, substrate binding; the displacement of a loop adjacent to the active, histidine brings previously overlooked residues into positions where they, may directly influence ... [(full description)]
About this StructureAbout this Structure
1E58 is a [Single protein] structure of sequence from [Escherichia coli] with SO4 and CL as [ligands]. The following page contains interesting information on the relation of 1E58 with [The Glycolytic Enzymes]. Active as [Phosphoglycerate mutase], with EC number [5.4.2.1]. Structure known Active Site: HIS. Full crystallographic information is available from [OCA].
ReferenceReference
High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase., Bond CS, White MF, Hunter WN, J Biol Chem. 2001 Feb 2;276(5):3247-53. Epub 2000 Oct 18. PMID:11038361
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