1m1b

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[[Image:1m1b.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate==
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|PDB= 1m1b |SIZE=350|CAPTION= <scene name='initialview01'>1m1b</scene>, resolution 2.25&Aring;
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<StructureSection load='1m1b' size='340' side='right'caption='[[1m1b]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene>
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<table><tr><td colspan='2'>[[1m1b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mytilus_edulis Mytilus edulis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M1B FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SPV:SULFOPYRUVATE'>SPV</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1b OCA], [https://pdbe.org/1m1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m1b RCSB], [https://www.ebi.ac.uk/pdbsum/1m1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m1b ProSAT]</span></td></tr>
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</table>
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'''Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate'''
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== Function ==
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[https://www.uniprot.org/uniprot/PEPM_MYTED PEPM_MYTED] Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr).
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m1/1m1b_consurf.spt"</scriptWhenChecked>
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1M1B 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=1M1B OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12162742 12162742]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m1b ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mytilus edulis]]
[[Category: Mytilus edulis]]
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[[Category: Phosphoenolpyruvate mutase]]
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[[Category: Dunaway-Mariano D]]
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[[Category: Single protein]]
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[[Category: Herzberg O]]
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[[Category: Dunaway-Mariano, D.]]
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[[Category: Jia Y]]
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[[Category: Herzberg, O.]]
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[[Category: Liu S]]
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[[Category: Jia, Y.]]
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[[Category: Lu Z]]
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[[Category: Liu, S.]]
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[[Category: Lu, Z.]]
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[[Category: MG]]
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[[Category: SPV]]
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[[Category: pep mutase]]
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[[Category: phosphoenolpyruvate mutase]]
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[[Category: sulfopyruvate]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:37:41 2008''
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Current revision

Crystal Structure of Phosphoenolpyruvate Mutase Complexed with Sulfopyruvate

PDB ID 1m1b

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