2v9y
From Proteopedia
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- | [[ | + | ==HUMAN AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE== |
+ | <StructureSection load='2v9y' size='340' side='right' caption='[[2v9y]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2v9y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V9Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V9Y FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mej|1mej]], [[1men|1men]], [[1meo|1meo]], [[1zly|1zly]], [[1njs|1njs]], [[1zlx|1zlx]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoribosylformylglycinamidine_cyclo-ligase Phosphoribosylformylglycinamidine cyclo-ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.3.1 6.3.3.1] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v9y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v9y RCSB], [http://www.ebi.ac.uk/pdbsum/2v9y PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == 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/v9/2v9y_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Human purine de novo synthesis pathway contains several multi-functional enzymes, one of which, tri-functional GART, contains three enzymatic activities in a single polypeptide chain. We have solved structures of two domains bearing separate catalytic functions: glycinamide ribonucleotide synthetase and aminoimidazole ribonucleotide synthetase. Structures are compared with those of homologous enzymes from prokaryotes and analyzed in terms of the catalytic mechanism. We also report small angle X-ray scattering models for the full-length protein. These models are consistent with the enzyme forming a dimer through the middle domain. The protein has an approximate seesaw geometry where terminal enzyme units display high mobility owing to flexible linker segments. This resilient seesaw shape may facilitate internal substrate/product transfer or forwarding to other enzymes in the pathway. | ||
- | + | Structural studies of tri-functional human GART.,Welin M, Grossmann JG, Flodin S, Nyman T, Stenmark P, Tresaugues L, Kotenyova T, Johansson I, Nordlund P, Lehtio L Nucleic Acids Res. 2010 Nov 1;38(20):7308-19. Epub 2010 Jul 14. PMID:20631005<ref>PMID:20631005</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phosphoribosylformylglycinamidine cyclo-ligase]] | [[Category: Phosphoribosylformylglycinamidine cyclo-ligase]] |
Revision as of 02:10, 1 October 2014
HUMAN AMINOIMIDAZOLE RIBONUCLEOTIDE SYNTHETASE
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Categories: Homo sapiens | Phosphoribosylformylglycinamidine cyclo-ligase | Arrowsmith, C H. | Berg, S Van Den. | Berglund, H. | Busam, R. | Collins, R. | Consortium, Structural Genomics. | Dahlgren, L G. | Edwards, A M. | Flodin, S. | Flores, A. | Graslund, S. | Hallberg, B M. | Hammarstrom, M. | Herman, M D. | Holmberg-Schiavone, L. | Johansson, I. | Kallas, A. | Karlberg, T. | Kotenyova, T. | Lehtio, L. | Moche, M. | Nordlund, P. | Nyman, T. | Persson, C. | Sagemark, J. | Stenmark, P. | Sundstrom, M. | Thorsell, A G. | Tresaugues, L. | Weigelt, J. | Welin, M. | Air | Aminoimidazole ribonucleotide synthetase | Atp-binding | Gart | Ligase | Multifunctional enzyme | Nucleotide-binding | Phosphorylation | Purine biosynthesis | Purine metabolism | Sgc | Structural genomic | Structural genomics consortium | Transferase