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| <StructureSection load='1r52' size='340' side='right'caption='[[1r52]], [[Resolution|resolution]] 2.89Å' scene=''> | | <StructureSection load='1r52' size='340' side='right'caption='[[1r52]], [[Resolution|resolution]] 2.89Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1r52]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R52 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R52 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1r52]] is a 4 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=1R52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R52 FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r53|1r53]]</div></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.89Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YGL148w ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1r52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r52 OCA], [https://pdbe.org/1r52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r52 RCSB], [https://www.ebi.ac.uk/pdbsum/1r52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r52 ProSAT]</span></td></tr> |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r52 OCA], [http://pdbe.org/1r52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r52 RCSB], [http://www.ebi.ac.uk/pdbsum/1r52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r52 ProSAT]</span></td></tr> | |
| </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=1r52 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=1r52 ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == 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>
| | ==See Also== |
| | | *[[Chorismate synthase|Chorismate synthase]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
| |
| <div class="pdbe-citations 1r52" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 18824]]
| |
| [[Category: Chorismate synthase]]
| |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Blondeau, K]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Bremang, M]] | | [[Category: Blondeau K]] |
| [[Category: Graille, M]] | | [[Category: Bremang M]] |
| [[Category: Janin, J]] | | [[Category: Graille M]] |
| [[Category: Leulliot, N]] | | [[Category: Janin J]] |
| [[Category: Meyer, P]] | | [[Category: Leulliot N]] |
| [[Category: Poupon, A]] | | [[Category: Meyer P]] |
| [[Category: Quevillon-Cheruel, S]] | | [[Category: Poupon A]] |
| [[Category: Sorel, I]] | | [[Category: Quevillon-Cheruel S]] |
| [[Category: Tilbeurgh, H van]] | | [[Category: Sorel I]] |
| [[Category: Lyase]]
| | [[Category: Van Tilbeurgh H]] |
| [[Category: Two layers alpha-beta]]
| |