From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1m1b.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1m1b.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1m1b| PDB=1m1b | SCENE= }} | | {{STRUCTURE_1m1b| PDB=1m1b | SCENE= }} |
| | | | |
| - | '''Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate'''
| + | ===Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The crystal structure of PEP mutase from Mytilus edulis in complex with a substrate-analogue inhibitor, sulfopyruvate S-pyr (K(i) = 22 microM), has been determined at 2.25 A resolution. Mg(II)-S-pyr binds in the alpha/beta barrel's central channel, at the C-termini of the beta-strands. The binding mode of S-pyr's pyruvyl moiety resembles the binding mode of oxalate seen earlier. The location of the sulfo group of S-pyr is postulated to mimic the phosphonyl group of the product phosphonopyruvate (P-pyr). This sulfo group interacts with the guanidinium group of Arg159, but it is not aligned for nucleopilic attack by neighboring basic amino side chains. Kinetic analysis of site directed mutants, probing the key active site residues Asp58, Arg159, Asn122, and His190 correlate well with the structural information. The results presented here rule out a phosphoryl transfer mechanism involving a double displacement, and suggest instead that PEP mutase catalysis proceeds via a dissociative mechanism in which the pyruvyl C(3) adds to the same face of the phosphorus from which the C(2)O departs. We propose that Arg159 and His190 serve to hold the phosphoryl/metaphosphate/phosphonyl group stationary along the reaction pathway, while the pyruvyl C(1)-C(2) bond rotates upon formation of the metaphosphate. In agreement with published data, the phosphoryl group transfer occurs on the Si-face of PEP with retention of configuration at phosphorus. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12162742}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12162742 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12162742}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Phosphoenolpyruvate mutase]] | | [[Category: Phosphoenolpyruvate mutase]] |
| | [[Category: Sulfopyruvate]] | | [[Category: Sulfopyruvate]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:30:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:00:01 2008'' |
Revision as of 20:00, 2 July 2008
Template:STRUCTURE 1m1b
Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate
Template:ABSTRACT PUBMED 12162742
About this Structure
1M1B is a Single protein structure of sequence from Mytilus edulis. Full crystallographic information is available from OCA.
Reference
Dissociative phosphoryl transfer in PEP mutase catalysis: structure of the enzyme/sulfopyruvate complex and kinetic properties of mutants., Liu S, Lu Z, Jia Y, Dunaway-Mariano D, Herzberg O, Biochemistry. 2002 Aug 13;41(32):10270-6. PMID:12162742
Page seeded by OCA on Wed Jul 2 23:00:01 2008
