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[[Image:1um0.jpg|left|200px]]
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{{STRUCTURE_1um0|  PDB=1um0  |  SCENE=  }}
'''Crystal structure of chorismate synthase complexed with FMN'''


==Crystal structure of chorismate synthase complexed with FMN==
<StructureSection load='1um0' size='340' side='right'caption='[[1um0]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROC_HELPY AROC_HELPY]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/um/1um0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1UM0 is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 1um0" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/15095868 15095868]
*[[Chorismate synthase|Chorismate synthase]]
[[Category: Chorismate synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ahn, H J.]]
[[Category: Ahn HJ]]
[[Category: Lee, B.]]
[[Category: Lee B]]
[[Category: Suh, S W.]]
[[Category: Suh SW]]
[[Category: Yoon, H J.]]
[[Category: Yoon HJ]]
[[Category: Beta-alpha-beta sandwich fold]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:24:39 2008''
Retrieved from "https://proteopedia.org/1um0"