1e58: Difference between revisions

Revision as of 14:40, 2 May 2008

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 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 StructureAbout 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.

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 Page seeded by OCA on Fri May 2 14:40:41 2008

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OCA

@@ Line 1: / Line 1: @@
 [[Image:1e58.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1e58 |SIZE=350|CAPTION= <scene name='initialview01'>1e58</scene>, resolution 1.25&Aring;
+The line below this paragraph, containing "STRUCTURE_1e58", creates the "Structure Box" on the page.
-|SITE= <scene name='pdbsite=HIS:Phosphohistidine'>HIS</scene>
+You may change the PDB parameter (which sets the PDB file loaded into the applet)
-|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE= PGM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
+-->
-|DOMAIN=
+{{STRUCTURE_1e58|  PDB=1e58  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e58 OCA], [http://www.ebi.ac.uk/pdbsum/1e58 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e58 RCSB]</span>
-}}
 '''E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE'''
@@ Line 29: / Line 26: @@
 [[Category: Bond, C S.]]
 [[Category: Hunter, W N.]]
-[[Category: glycolysis and gluconeogenesis]]
+[[Category: Glycolysis and gluconeogenesis]]
-[[Category: isomerase]]
+[[Category: Isomerase]]
-[[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 Sun Mar 30 19:55:29 2008''