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[[Image:1r53.jpg|left|200px]]<br /><applet load="1r53" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1r53, resolution 2.20&Aring;" />
'''Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae'''<br />


==Overview==
==Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae==
Chorismate synthase (EC 4.2.3.5), the seventh enzyme in the shikimate pathway, catalyzes the transformation of 5-enolpyruvylshikimate 3-phosphate (EPSP) to chorismate, which is the last common precursor in the biosynthesis of numerous aromatic compounds in bacteria, fungi, and plants. The chorismate synthase reaction involves a 1,4-trans-elimination of phosphoric acid from EPSP and has an absolute requirement for reduced FMN as a cofactor. We have determined the three-dimensional x-ray structure of the yeast chorismate synthase from selenomethionine-labeled crystals at 2.2-A resolution. The structure shows a novel betaalphabetaalpha fold consisting of an alternate tight packing of two alpha-helical and two beta-sheet layers, showing no resemblance to any documented protein structure. The molecule is arranged as a tight tetramer with D2 symmetry, in accordance with its quaternary structure in solution. Electron density is missing for 23% of the amino acids, spread over sequence regions that in the three-dimensional structure converge on the surface of the protein. Many totally conserved residues are contained within these regions, and they probably form a structured but mobile domain that closes over a cleft upon substrate binding and catalysis. This hypothesis is supported by previously published spectroscopic measurements implying that the enzyme undergoes considerable structural changes upon binding of both FMN and EPSP.
<StructureSection load='1r53' size='340' side='right'caption='[[1r53]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1r53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R53 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]] 2.2&#8491;</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=1r53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r53 OCA], [https://pdbe.org/1r53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r53 RCSB], [https://www.ebi.ac.uk/pdbsum/1r53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r53 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AROC_YEAST AROC_YEAST]
== 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/r5/1r53_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=1r53 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1R53 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1R53 OCA].
*[[Chorismate synthase|Chorismate synthase]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae., Quevillon-Cheruel S, Leulliot N, Meyer P, Graille M, Bremang M, Blondeau K, Sorel I, Poupon A, Janin J, van Tilbeurgh H, J Biol Chem. 2004 Jan 2;279(1):619-25. Epub 2003 Oct 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14573601 14573601]
[[Category: Large Structures]]
[[Category: Chorismate synthase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Blondeau K]]
[[Category: Blondeau, K.]]
[[Category: Bremang M]]
[[Category: Bremang, M.]]
[[Category: Graille M]]
[[Category: Graille, M.]]
[[Category: Janin J]]
[[Category: Janin, J.]]
[[Category: Leulliot N]]
[[Category: Leulliot, N.]]
[[Category: Meyer P]]
[[Category: Meyer, P.]]
[[Category: Poupon A]]
[[Category: Poupon, A.]]
[[Category: Quevillon-Cheruel S]]
[[Category: Quevillon-Cheruel, S.]]
[[Category: Sorel I]]
[[Category: Sorel, I.]]
[[Category: Van Tilbeurgh H]]
[[Category: Tilbeurgh, H van.]]
[[Category: two layers alpha-beta]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:08 2008''
Retrieved from "https://proteopedia.org/1r53"