1iug
From Proteopedia
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- | [[ | + | ==The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus== |
+ | <StructureSection load='1iug' size='340' side='right' caption='[[1iug]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1iug]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IUG FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></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=1iug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iug OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1iug RCSB], [http://www.ebi.ac.uk/pdbsum/1iug PDBsum], [http://www.topsan.org/Proteins/RSGI/1iug TOPSAN]</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/iu/1iug_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 == | ||
+ | Protein TT0402 from Thermus thermophilus HB8 exhibits about 30-35% sequence identity with proteins belonging to subgroup IV in the aminotransferase family of the fold-type I pyridoxal 5'-phosphate (PLP)-dependent enzymes. In this study, we determined the crystal structure of TT0402 at 2.3 A resolution (R(factor) = 19.9%, R(free) = 23.6%). The overall structure of TT0402 exhibits the fold conserved in aminotransferases, and is most similar to that of the Escherichia coli phosphoserine aminotransferase, which belongs to subgroup IV but shares as little as 13% sequence identity with TT0402. Kinetic assays confirmed that TT0402 has higher transamination activities with the amino group donor, L-glutamate, and somewhat lower activities with L-aspartate. These results indicate that TT0402 is a subgroup IV aminotransferase for the synthesis/degradation of either L-aspartate or a similar compound. | ||
- | + | Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV.,Katsura Y, Shirouzu M, Yamaguchi H, Ishitani R, Nureki O, Kuramitsu S, Hayashi H, Yokoyama S Proteins. 2004 May 15;55(3):487-92. PMID:15103612<ref>PMID:15103612</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | == | + | |
- | < | + | |
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Hayashi, H.]] | [[Category: Hayashi, H.]] |
Revision as of 08:55, 28 September 2014
The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus
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Categories: Thermus thermophilus | Hayashi, H. | Ishitani, R. | Katsura, Y. | Kuramitsu, S. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirouzu, M. | Yamaguchi, H. | Yokoyama, S. | Pyridoxal-5'-phosphate form | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Transferase | Wild type