5vht
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli chorismate mutase with orthogonal interface containing p-benzoyl phenylalanine== | |
| + | <StructureSection load='5vht' size='340' side='right' caption='[[5vht]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vht]] is a 2 chain structure. 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> | ||
| + | </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> | ||
| + | <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'>[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> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28413876</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5vht" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chorismate mutase]] | ||
| + | [[Category: Han, G W]] | ||
| + | [[Category: Koh, M]] | ||
| + | [[Category: Nasertorabi, F]] | ||
| + | [[Category: Shultz, P G]] | ||
| + | [[Category: Stevens, R C]] | ||
| + | [[Category: Isomerase]] | ||
| + | [[Category: Mutagenesis]] | ||
| + | [[Category: Orthogonal interface]] | ||
| + | [[Category: P-benzoyl phenylalanine]] | ||
Revision as of 12:49, 10 May 2017
E. coli chorismate mutase with orthogonal interface containing p-benzoyl phenylalanine
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