1r53

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[[Image:1r53.jpg|left|200px]]
 
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==Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae==
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The line below this paragraph, containing "STRUCTURE_1r53", creates the "Structure Box" on the page.
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<StructureSection load='1r53' size='340' side='right'caption='[[1r53]], [[Resolution|resolution]] 2.20&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'>[[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>
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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]] 2.2&#8491;</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=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>
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{{STRUCTURE_1r53| PDB=1r53 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AROC_YEAST AROC_YEAST]
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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/r5/1r53_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=1r53 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae'''
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==See Also==
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*[[Chorismate synthase|Chorismate synthase]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Large Structures]]
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==About this Structure==
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1R53 is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14573601 14573601]
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[[Category: Chorismate synthase]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Blondeau K]]
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[[Category: Blondeau, K.]]
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[[Category: Bremang M]]
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[[Category: Bremang, M.]]
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[[Category: Graille M]]
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[[Category: Graille, M.]]
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[[Category: Janin J]]
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[[Category: Janin, J.]]
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[[Category: Leulliot N]]
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[[Category: Leulliot, N.]]
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[[Category: Meyer P]]
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[[Category: Meyer, P.]]
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[[Category: Poupon A]]
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[[Category: Poupon, A.]]
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[[Category: Quevillon-Cheruel S]]
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[[Category: Quevillon-Cheruel, S.]]
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[[Category: Sorel I]]
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[[Category: Sorel, I.]]
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[[Category: Van Tilbeurgh H]]
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[[Category: Tilbeurgh, H van.]]
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[[Category: Two layers alpha-beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:05:10 2008''
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Current revision

Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae

PDB ID 1r53

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