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==A re-refinement of the isochorismate synthase EntC==
==A re-refinement of the isochorismate synthase EntC==
<StructureSection load='5jzd' size='340' side='right' caption='[[5jzd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5jzd' size='340' side='right'caption='[[5jzd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5jzd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JZD FirstGlance]. <br>
<table><tr><td colspan='2'>[[5jzd]] 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=5JZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JZD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ISC:(5S,6S)-5-[(1-CARBOXYETHENYL)OXY]-6-HYDROXYCYCLOHEXA-1,3-DIENE-1-CARBOXYLIC+ACID'>ISC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.303&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hwo|3hwo]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ISC:(5S,6S)-5-[(1-CARBOXYETHENYL)OXY]-6-HYDROXYCYCLOHEXA-1,3-DIENE-1-CARBOXYLIC+ACID'>ISC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isochorismate_synthase Isochorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.4.2 5.4.4.2] </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=5jzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jzd OCA], [https://pdbe.org/5jzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jzd RCSB], [https://www.ebi.ac.uk/pdbsum/5jzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jzd 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=5jzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jzd OCA], [http://pdbe.org/5jzd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jzd RCSB], [http://www.ebi.ac.uk/pdbsum/5jzd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jzd ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/ENTC_ECOLI ENTC_ECOLI]
EntC, one of two isochorismate synthases in Escherichia coli, is specific to the biosynthesis of the siderophore enterobactin. Here, we report the crystal structure of EntC in complex with isochorismate and Mg(2+)at 2.3 A resolution, the first structure of a chorismate-utilizing enzyme with a non-aromatic reaction product. EntC exhibits a complex alpha+beta fold like the other chorismate-utilizing enzymes, such as salicylate synthase and anthranilate synthase. Comparison of active site structures allowed the identification of several residues, not discussed previously, that might be important for the isochorismate activity of the EntC. Although EntC, MenF and Irp9 all convert chorismate to isochorismate, only Irp9 subsequently exhibits isochorismate pyruvate lyase activity resulting in the formation of salicylate and pyruvate as the reaction products. With a view to understanding the roles of these amino acid residues in the conversion of chorismate to isochorismate and to obtaining clues about the pyruvate lyase activity of Irp9, several mutants of EntC were generated in which the selected residues in EntC were substituted for those of Irp9: these included A303T, L304A, F327Y, I346L and F359Q mutations. Biochemical analysis of these mutants indicated that the side chain of A303 in EntC may be crucial in the orientation of the carbonyl to allow formation of a hydrogen bond with isochorismate. Some mutations, such as L304A and F359Q, give rise to a loss of catalytic activity, whereas others, such as F327Y and I346L, show that subtle changes in the otherwise closely similar active sites influence activity. We did not find a combination of these residues that conferred pyruvate lyase activity.
 
Crystal structure of Escherichia coli enterobactin-specific isochorismate synthase (EntC) bound to its reaction product isochorismate: implications for the enzyme mechanism and differential activity of chorismate-utilizing enzymes.,Sridharan S, Howard N, Kerbarh O, Blaszczyk M, Abell C, Blundell TL J Mol Biol. 2010 Mar 19;397(1):290-300. Epub 2010 Jan 15. PMID:20079748<ref>PMID:20079748</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jzd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Isochorismate synthase]]
[[Category: Escherichia coli K-12]]
[[Category: Lamb, A L]]
[[Category: Large Structures]]
[[Category: Meneely, K M]]
[[Category: Lamb AL]]
[[Category: Chorismate]]
[[Category: Meneely KM]]
[[Category: Isochorismate]]
[[Category: Isomerase]]

Latest revision as of 15:38, 6 March 2024

A re-refinement of the isochorismate synthase EntCA re-refinement of the isochorismate synthase EntC

Structural highlights

5jzd is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.303Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENTC_ECOLI

5jzd, resolution 2.30Å

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