1iug

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(New page: 200px<br /><applet load="1iug" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iug, resolution 2.2&Aring;" /> '''The crystal structure...)
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[[Image:1iug.jpg|left|200px]]<br /><applet load="1iug" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1iug, resolution 2.2&Aring;" />
 
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'''The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus'''<br />
 
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==Overview==
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==The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus==
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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.
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<StructureSection load='1iug' size='340' side='right'caption='[[1iug]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1iug]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1IUG FirstGlance]. <br>
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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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1iug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iug OCA], [https://pdbe.org/1iug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iug RCSB], [https://www.ebi.ac.uk/pdbsum/1iug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iug ProSAT], [https://www.topsan.org/Proteins/RSGI/1iug TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/P83786_THETH P83786_THETH]
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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/iu/1iug_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1iug ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1IUG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IUG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15103612 15103612]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1iug" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: Hayashi, H.]]
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[[Category: Hayashi H]]
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[[Category: Ishitani, R.]]
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[[Category: Ishitani R]]
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[[Category: Katsura, Y.]]
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[[Category: Katsura Y]]
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[[Category: Kuramitsu, S.]]
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[[Category: Kuramitsu S]]
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[[Category: Nureki, O.]]
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[[Category: Nureki O]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: Shirouzu M]]
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[[Category: Shirouzu, M.]]
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[[Category: Yamaguchi H]]
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[[Category: Yamaguchi, H.]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S.]]
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[[Category: PO4]]
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[[Category: pyridoxal-5'-phosphate form]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: wild type]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:33:48 2007''
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Current revision

The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus

PDB ID 1iug

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