1um0

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(New page: 200px<br /><applet load="1um0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1um0, resolution 1.95&Aring;" /> '''Crystal structure of...)
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[[Image:1um0.jpg|left|200px]]<br /><applet load="1um0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1um0, resolution 1.95&Aring;" />
 
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'''Crystal structure of chorismate synthase complexed with FMN'''<br />
 
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==Overview==
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==Crystal structure of chorismate synthase complexed with FMN==
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Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate, 3-phosphate to chorismate in the shikimate pathway, which represents an, attractive target for discovering antimicrobial agents and herbicides., Chorismate serves as a common precursor for the synthesis of aromatic, amino acids and many aromatic compounds in microorganisms and plants., Chorismate synthase requires reduced FMN as a cofactor but the catalyzed, reaction involves no net redox change. Here, we have determined the, crystal structure of chorismate synthase from Helicobacter pylori in both, FMN-bound and FMN-free forms. It is a tetrameric enzyme, with each monomer, possessing a novel "beta-alpha-beta sandwich fold". Highly conserved, regions, including several flexible loops, cluster together around the, bound FMN to form the active site. The unique FMN-binding site is formed, largely by a single subunit, with a small contribution from a neighboring, subunit. The isoalloxazine ring of the bound FMN is significantly, non-planar. Our structure illuminates the essential functional roles, played by the cofactor.
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<StructureSection load='1um0' size='340' side='right'caption='[[1um0]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1um0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UM0 FirstGlance]. <br>
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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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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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=1um0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1um0 OCA], [https://pdbe.org/1um0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1um0 RCSB], [https://www.ebi.ac.uk/pdbsum/1um0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1um0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AROC_HELPY AROC_HELPY]
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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/um/1um0_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=1um0 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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Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate to chorismate in the shikimate pathway, which represents an attractive target for discovering antimicrobial agents and herbicides. Chorismate serves as a common precursor for the synthesis of aromatic amino acids and many aromatic compounds in microorganisms and plants. Chorismate synthase requires reduced FMN as a cofactor but the catalyzed reaction involves no net redox change. Here, we have determined the crystal structure of chorismate synthase from Helicobacter pylori in both FMN-bound and FMN-free forms. It is a tetrameric enzyme, with each monomer possessing a novel "beta-alpha-beta sandwich fold". Highly conserved regions, including several flexible loops, cluster together around the bound FMN to form the active site. The unique FMN-binding site is formed largely by a single subunit, with a small contribution from a neighboring subunit. The isoalloxazine ring of the bound FMN is significantly non-planar. Our structure illuminates the essential functional roles played by the cofactor.
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==About this Structure==
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Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights.,Ahn HJ, Yoon HJ, Lee B 2nd, Suh SW J Mol Biol. 2004 Feb 27;336(4):903-15. PMID:15095868<ref>PMID:15095868</ref>
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1UM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chorismate_synthase Chorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.5 4.2.3.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UM0 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights., Ahn HJ, Yoon HJ, Lee B 2nd, Suh SW, J Mol Biol. 2004 Feb 27;336(4):903-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15095868 15095868]
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</div>
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[[Category: Chorismate synthase]]
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<div class="pdbe-citations 1um0" style="background-color:#fffaf0;"></div>
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[[Category: Helicobacter pylori]]
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[[Category: Single protein]]
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[[Category: Ahn, H.J.]]
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[[Category: Lee, B.]]
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[[Category: Suh, S.W.]]
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[[Category: Yoon, H.J.]]
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[[Category: FMN]]
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[[Category: beta-alpha-beta sandwich fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:14:07 2007''
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==See Also==
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*[[Chorismate synthase|Chorismate synthase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Helicobacter pylori]]
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[[Category: Large Structures]]
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[[Category: Ahn HJ]]
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[[Category: Lee B]]
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[[Category: Suh SW]]
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[[Category: Yoon HJ]]

Current revision

Crystal structure of chorismate synthase complexed with FMN

PDB ID 1um0

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