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| - | [[Image:1s2v.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1s2v| PDB=1s2v | SCENE= }} | | {{STRUCTURE_1s2v| PDB=1s2v | SCENE= }} |
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| - | '''Crystal structure of phosphoenolpyruvate mutase complexed with Mg(II)'''
| + | ===Crystal structure of phosphoenolpyruvate mutase complexed with Mg(II)=== |
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| - | ==Overview==
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| - | Previous work has indicated that PEP mutase catalyzes the rearrangement of phosphoenolpyruvate to phosphonopyruvate by a dissociative mechanism. The crystal structure of the mutase with Mg(II) and sulfopyruvate (a phosphonopyruvate analogue) bound showed that the substrate is anchored to the active site by the Mg(II), and shielded from solvent by a large loop (residues 115-133). Here, the crystal structures of wild-type and D58A mutases, in the apo state and in complex with Mg(II), are reported. In both unbound and Mg(II)-bound states, the active site is accessible to the solvent. The loop (residues 115-133), which in the enzyme-inhibitor complexes covers the active site cavity, is partially disordered or adopts a conformation that allows access to the cavity. In the apo state, the residues associated with Mg(II) binding are poised to accept the metal ion. When Mg(II) binds, the coordination is the same as that previously observed in the enzyme-Mg(II) sulfopyruvate complex, except that the coordination positions occupied by two ligand oxygen atoms are occupied by two water molecules. When the loop opens, three key active site residues are displaced from the active site, Lys120, Asn122, and Leu124. Lys120 mediates Mg(II) coordination. Asn122 and Leu124 surround the transferring phosphoryl group, and thus prevent substrate hydrolysis. Amino acid replacement of any one of these three loop residues results in a significant loss of catalytic activity. It is hypothesized that the loop serves to gate the mutase active site, interconverting between an open conformation that allows substrate binding and product release and a closed conformation that separates the reaction site from the solvent during catalysis.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15078090}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15078090 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15078090}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Phosphonopyruvate]] | | [[Category: Phosphonopyruvate]] |
| | [[Category: X-ray structure]] | | [[Category: X-ray structure]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:13:44 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:53:10 2008'' |
Revision as of 09:53, 29 July 2008
Template:STRUCTURE 1s2v
Crystal structure of phosphoenolpyruvate mutase complexed with Mg(II)
Template:ABSTRACT PUBMED 15078090
About this Structure
1S2V is a Single protein structure of sequence from Mytilus edulis. Full crystallographic information is available from OCA.
Reference
Conformational flexibility of PEP mutase., Liu S, Lu Z, Han Y, Jia Y, Howard A, Dunaway-Mariano D, Herzberg O, Biochemistry. 2004 Apr 20;43(15):4447-53. PMID:15078090
Page seeded by OCA on Tue Jul 29 12:53:10 2008
