1pym
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1pym.jpg|left|200px]] | + | [[Image:1pym.jpg|left|200px]] |
| - | + | ||
| - | '''PHOSPHOENOLPYRUVATE MUTASE FROM MOLLUSK IN WITH BOUND MG2-OXALATE''' | + | {{Structure |
| + | |PDB= 1pym |SIZE=350|CAPTION= <scene name='initialview01'>1pym</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoenolpyruvate_mutase Phosphoenolpyruvate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.9 5.4.2.9] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PHOSPHOENOLPYRUVATE MUTASE FROM MOLLUSK IN WITH BOUND MG2-OXALATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1PYM is a [ | + | 1PYM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYM OCA]. |
==Reference== | ==Reference== | ||
| - | Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate., Huang K, Li Z, Jia Y, Dunaway-Mariano D, Herzberg O, Structure. 1999 May;7(5):539-48. PMID:[http:// | + | Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate., Huang K, Li Z, Jia Y, Dunaway-Mariano D, Herzberg O, Structure. 1999 May;7(5):539-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10378273 10378273] |
[[Category: Mytilus edulis]] | [[Category: Mytilus edulis]] | ||
[[Category: Phosphoenolpyruvate mutase]] | [[Category: Phosphoenolpyruvate mutase]] | ||
| Line 23: | Line 32: | ||
[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:30:40 2008'' |
Revision as of 11:30, 20 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Phosphoenolpyruvate mutase, with EC number 5.4.2.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PHOSPHOENOLPYRUVATE MUTASE FROM MOLLUSK IN WITH BOUND MG2-OXALATE
Overview
BACKGROUND: Phosphonate compounds are important secondary metabolites in nature and, when linked to macromolecules in eukaryotes, they might play a role in cell signaling. The first obligatory step in the biosynthesis of phosphonates is the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-pyr), a reaction that is catalyzed by PEP mutase. The PEP mutase functions as a tetramer and requires magnesium ions (Mg2+). RESULTS: The crystal structure of PEP mutase from the mollusk Mytilus edulis, bound to the inhibitor Mg(2+)-oxalate, has been determined using multiwavelength anomalous diffraction, exploiting the selenium absorption edge of a selenomethionine-containing protein. The structure has been refined at 1.8 A resolution. PEP mutase adopts a modified alpha/beta barrel fold, in which the eighth alpha helix projects away from the alpha/beta barrel instead of packing against the beta sheet. A tightly associated dimer is formed, such that the two eighth helices are swapped, each packing against the beta sheet of the neighboring molecule. A dimer of dimers further associates into a tetramer. Mg(2+)-oxalate is buried close to the center of the barrel, at the C-terminal ends of the beta strands. CONCLUSIONS: The tetramer observed in the crystal is likely to be physiologically relevant. Because the Mg(2+)-oxalate is inaccessible to solvent, substrate binding and dissociation might be accompanied by conformational changes. A mechanism involving a phosphoenzyme intermediate is proposed, with Asp58 acting as the nucleophilic entity that accepts and delivers the phosphoryl group. The active-site architecture and the chemistry performed by PEP mutase are different from other alpha/beta-barrel proteins that bind pyruvate or PEP, thus the enzyme might represent a new family of alpha/beta-barrel proteins.
About this Structure
1PYM is a Single protein structure of sequence from Mytilus edulis. Full crystallographic information is available from OCA.
Reference
Helix swapping between two alpha/beta barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg(2+)-oxalate., Huang K, Li Z, Jia Y, Dunaway-Mariano D, Herzberg O, Structure. 1999 May;7(5):539-48. PMID:10378273
Page seeded by OCA on Thu Mar 20 13:30:40 2008
