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| | <StructureSection load='2gtv' size='340' side='right'caption='[[2gtv]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | | <StructureSection load='2gtv' size='340' side='right'caption='[[2gtv]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2gtv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GTV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2gtv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GTV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TSA:8-HYDROXY-2-OXA-BICYCLO[3.3.1]NON-6-ENE-3,5-DICARBOXYLIC+ACID'>TSA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gtv OCA], [http://pdbe.org/2gtv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gtv RCSB], [http://www.ebi.ac.uk/pdbsum/2gtv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gtv ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gtv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gtv OCA], [https://pdbe.org/2gtv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gtv RCSB], [https://www.ebi.ac.uk/pdbsum/2gtv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gtv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHMU_METJA CHMU_METJA]] Catalyzes the conversion of chorismate into prephenate via a Claisen rearrangement.<ref>PMID:9665711</ref> | + | [[https://www.uniprot.org/uniprot/CHMU_METJA CHMU_METJA]] Catalyzes the conversion of chorismate into prephenate via a Claisen rearrangement.<ref>PMID:9665711</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Function
[CHMU_METJA] Catalyzes the conversion of chorismate into prephenate via a Claisen rearrangement.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Although protein dynamics has been recognized as a potentially important contributor to enzyme catalysis, structural disorder is generally considered to reduce catalytic efficiency. This widely held assumption has recently been challenged by the finding that an engineered chorismate mutase combines high catalytic activity with the properties of a molten globule, a loosely packed and highly dynamic conformational ensemble. Taking advantage of the ordering observed upon ligand binding, we have now used NMR spectroscopy to characterize this enzyme in complex with a transition-state analog. The complex adopts a helix-bundle structure, as designed, but retains unprecedented flexibility on the millisecond timescale across its entire length. Moreover, pre-steady-state kinetics data show that binding occurs by an induced-fit mechanism on the same timescale as the enzymatic reaction, linking global conformational plasticity with efficient catalysis.
Structure and dynamics of a molten globular enzyme.,Pervushin K, Vamvaca K, Vogeli B, Hilvert D Nat Struct Mol Biol. 2007 Dec;14(12):1202-6. Epub 2007 Nov 11. PMID:17994104[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ MacBeath G, Kast P, Hilvert D. A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii. Biochemistry. 1998 Jul 14;37(28):10062-73. PMID:9665711 doi:http://dx.doi.org/10.1021/bi980449t
- ↑ Pervushin K, Vamvaca K, Vogeli B, Hilvert D. Structure and dynamics of a molten globular enzyme. Nat Struct Mol Biol. 2007 Dec;14(12):1202-6. Epub 2007 Nov 11. PMID:17994104 doi:http://dx.doi.org/10.1038/nsmb1325
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