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| | <StructureSection load='5vht' size='340' side='right'caption='[[5vht]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5vht' size='340' side='right'caption='[[5vht]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vht]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VHT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VHT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vht]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VHT FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PBF:PARA-(BENZOYL)-PHENYLALANINE'>PBF</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pheA, b2599, JW2580 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PBF:PARA-(BENZOYL)-PHENYLALANINE'>PBF</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5vht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vht OCA], [https://pdbe.org/5vht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vht RCSB], [https://www.ebi.ac.uk/pdbsum/5vht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vht ProSAT]</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=5vht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vht OCA], [http://pdbe.org/5vht PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vht RCSB], [http://www.ebi.ac.uk/pdbsum/5vht PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vht ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHEA_ECOLI PHEA_ECOLI]] Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.<ref>PMID:4261395</ref> | + | [https://www.uniprot.org/uniprot/CMPDT_ECOLI CMPDT_ECOLI] Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.<ref>PMID:4261395</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5vht" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5vht" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[3D structures of chorismate mutase|3D structures of chorismate mutase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chorismate mutase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Han, G W]] | + | [[Category: Han GW]] |
| - | [[Category: Koh, M]] | + | [[Category: Koh M]] |
| - | [[Category: Nasertorabi, F]] | + | [[Category: Nasertorabi F]] |
| - | [[Category: Shultz, P G]] | + | [[Category: Shultz PG]] |
| - | [[Category: Stevens, R C]] | + | [[Category: Stevens RC]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Mutagenesis]]
| + | |
| - | [[Category: Orthogonal interface]]
| + | |
| - | [[Category: P-benzoyl phenylalanine]]
| + | |
| Structural highlights
Function
CMPDT_ECOLI Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.[1]
Publication Abstract from PubMed
We have engineered the protein interface of the Escherichia coli chorismate mutase (EcCM) homodimer to be dependent on incorporation of a noncanonical amino acid (ncAA) at residue 72. The large hydrophobic amino acid p-benzoyl phenylalanine (pBzF) was substituted for Tyr72, which led to a catalytically inactive protein. A library of five residues (Leu25', Arg29', Leu76, Ile80' and Asp83') surrounding pBzF72 was generated and subjected to a growth based selection in a chorismate mutase deficient strain. An EcCM variant (Phe25', pBzF72, Thr76, Gly80' and Tyr83') forms a stable homodimer, has catalytic activity similar to the wild type enzyme, and unfolds with a Tm of 53 degrees C. The X-ray crystal structure reveals a pi-pi stacking and hydrogen bonding interactions that stabilize the new protein interface. The strategy described here should be useful for generating organisms that are dependent on the presence of a ncAA for growth.
Generation of an Orthogonal Protein-Protein Interface with a Noncanonical Amino Acid.,Koh M, Nasertorabi F, Han GW, Stevens RC, Schultz PG J Am Chem Soc. 2017 Apr 26;139(16):5728-5731. doi: 10.1021/jacs.7b02273. Epub, 2017 Apr 17. PMID:28413876[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dopheide TA, Crewther P, Davidson BE. Chorismate mutase-prephenate dehydratase from Escherichia coli K-12. II. Kinetic properties. J Biol Chem. 1972 Jul 25;247(14):4447-52. PMID:4261395
- ↑ Koh M, Nasertorabi F, Han GW, Stevens RC, Schultz PG. Generation of an Orthogonal Protein-Protein Interface with a Noncanonical Amino Acid. J Am Chem Soc. 2017 Apr 26;139(16):5728-5731. doi: 10.1021/jacs.7b02273. Epub, 2017 Apr 17. PMID:28413876 doi:http://dx.doi.org/10.1021/jacs.7b02273
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