1e58: Difference between revisions

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[[Image:1e58.gif|left|200px]]
[[Image:1e58.png|left|200px]]


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==Overview==
{{ABSTRACT_11038361}}
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 catalysis. E. coli dPGM, like the mammalian dPGMs, is a dimer, whereas previous structural work has concentrated on monomeric and tetrameric yeast forms. We can now analyze the sequence differences that cause this variation of quaternary structure.


==About this Structure==
==About this Structure==
1E58 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E58 OCA].  
1E58 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E58 OCA].  
==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://www.ncbi.nlm.nih.gov/pubmed/11038361 11038361]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Phosphoglycerate mutase]]
[[Category: Phosphoglycerate mutase]]
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[[Category: Phosphoglycerate mutase]]
[[Category: Phosphoglycerate mutase]]
[[Category: Phosphohistidine]]
[[Category: Phosphohistidine]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:40:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 17:12:14 2008''

Revision as of 14:12, 26 June 2008

File:1e58.png

Template:STRUCTURE 1e58

E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE


Template:ABSTRACT 11038361

About this Structure

1E58 is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1E58 with [The Glycolytic Enzymes]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 17:12:14 2008

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