1r53
From Proteopedia
(Difference between revisions)
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<StructureSection load='1r53' size='340' side='right'caption='[[1r53]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1r53' size='340' side='right'caption='[[1r53]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1r53]] is a 1 chain structure with sequence from [ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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> | |
- | + | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/AROC_YEAST AROC_YEAST] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1r53 ConSurf]. | </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> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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. | ||
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- | 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:14573601<ref>PMID:14573601</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1r53" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Chorismate synthase|Chorismate synthase]] | *[[Chorismate synthase|Chorismate synthase]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Atcc 18824]] | ||
- | [[Category: Chorismate synthase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Blondeau | + | [[Category: Saccharomyces cerevisiae]] |
- | [[Category: Bremang | + | [[Category: Blondeau K]] |
- | [[Category: Graille | + | [[Category: Bremang M]] |
- | [[Category: Janin | + | [[Category: Graille M]] |
- | [[Category: Leulliot | + | [[Category: Janin J]] |
- | [[Category: Meyer | + | [[Category: Leulliot N]] |
- | [[Category: Poupon | + | [[Category: Meyer P]] |
- | [[Category: Quevillon-Cheruel | + | [[Category: Poupon A]] |
- | [[Category: Sorel | + | [[Category: Quevillon-Cheruel S]] |
- | [[Category: Tilbeurgh | + | [[Category: Sorel I]] |
- | + | [[Category: Van Tilbeurgh H]] | |
- | + |
Current revision
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae
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