View source for 5vht


==E. coli chorismate mutase with orthogonal interface containing p-benzoyl phenylalanine==
<StructureSection load='5vht' size='340' side='right'caption='[[5vht]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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='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>
</table>
== Function ==
[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;">
== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</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/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Han GW]]
[[Category: Koh M]]
[[Category: Nasertorabi F]]
[[Category: Shultz PG]]
[[Category: Stevens RC]]