3nvt

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[[Image:3nvt.png|left|200px]]
 
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==1.95 Angstrom crystal structure of a bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase (aroA) from Listeria monocytogenes EGD-e==
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The line below this paragraph, containing "STRUCTURE_3nvt", creates the "Structure Box" on the page.
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<StructureSection load='3nvt' size='340' side='right'caption='[[3nvt]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3nvt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NVT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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{{STRUCTURE_3nvt| PDB=3nvt | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nvt OCA], [https://pdbe.org/3nvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nvt RCSB], [https://www.ebi.ac.uk/pdbsum/3nvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nvt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8Y6T2_LISMO Q8Y6T2_LISMO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/3nvt_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3nvt ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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3-Deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS) catalyzes the first step in the biosynthesis of a number of aromatic metabolites. Likely because this reaction is situated at a pivotal biosynthetic gateway, several DAHPS classes distinguished by distinct mechanisms of allosteric regulation have independently evolved. One class of DAHPSs contains a regulatory domain with sequence homology to chorismate mutase-an enzyme further downstream of DAHPS that catalyzes the first committed step in tyrosine/phenylalanine biosynthesis-and is inhibited by chorismate mutase substrate (chorismate) and product (prephenate). Described in this work, structures of the Listeria monocytogenes chorismate/prephenate regulated DAHPS in complex with Mn(2+) and Mn(2+) + phosphoenolpyruvate reveal an unusual quaternary architecture: DAHPS domains assemble as a tetramer, from either side of which chorismate mutase-like (CML) regulatory domains asymmetrically emerge to form a pair of dimers. This domain organization suggests that chorismate/prephenate binding promotes a stable interaction between the discrete regulatory and catalytic domains and supports a mechanism of allosteric inhibition similar to tyrosine/phenylalanine control of a related DAHPS class. We argue that the structural similarity of chorismate mutase enzyme and CML regulatory domain provides a unique opportunity for the design of a multitarget antibacterial.
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===1.95 Angstrom crystal structure of a bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase (aroA) from Listeria monocytogenes EGD-e===
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Structural analysis of a 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase with an N-terminal chorismate mutase-like regulatory domain.,Light SH, Halavaty AS, Minasov G, Shuvalova L, Anderson WF Protein Sci. 2012 Apr 13. doi: 10.1002/pro.2075. PMID:22505283<ref>PMID:22505283</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3nvt" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_22505283}}, adds the Publication Abstract to the page
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*[[DAHP synthase 3D structures|DAHP synthase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22505283 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22505283}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3nvt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVT OCA].
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[[Category: Listeria monocytogenes EGD-e]]
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[[Category: Anderson WF]]
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==Reference==
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[[Category: Halavaty AS]]
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<ref group="xtra">PMID:022505283</ref><references group="xtra"/>
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[[Category: Kwon K]]
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[[Category: Listeria monocytogenes]]
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[[Category: Light SH]]
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[[Category: Anderson, W F.]]
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[[Category: Minasov G]]
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[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
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[[Category: Shuvalova L]]
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[[Category: Halavaty, A S.]]
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[[Category: Kwon, K.]]
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[[Category: Light, S H.]]
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[[Category: Minasov, G.]]
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[[Category: Shuvalova, L.]]
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[[Category: Amino acid biosynthesis]]
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[[Category: Bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase]]
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[[Category: Center for structural genomics of infectious disease]]
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[[Category: Csgid]]
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[[Category: Infectious disease]]
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[[Category: Listeria monocytogenes egd-e]]
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[[Category: Structural genomic]]
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[[Category: Tim barrel]]
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[[Category: Transferase]]
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[[Category: Transferase-isomerase complex]]
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Current revision

1.95 Angstrom crystal structure of a bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase (aroA) from Listeria monocytogenes EGD-e

PDB ID 3nvt

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