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1bjw

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[[Image:1bjw.jpg|left|200px]]
 
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==ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS==
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The line below this paragraph, containing "STRUCTURE_1bjw", creates the "Structure Box" on the page.
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<StructureSection load='1bjw' size='340' side='right'caption='[[1bjw]], [[Resolution|resolution]] 1.80&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'>[[1bjw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BJW 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]] 1.8&#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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{{STRUCTURE_1bjw| PDB=1bjw | SCENE= }}
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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=1bjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bjw OCA], [https://pdbe.org/1bjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bjw RCSB], [https://www.ebi.ac.uk/pdbsum/1bjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bjw ProSAT], [https://www.topsan.org/Proteins/RSGI/1bjw TOPSAN]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AAPAT_THET8 AAPAT_THET8] Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).<ref>PMID:25070637</ref> <ref>PMID:30771275</ref> <ref>PMID:8907187</ref>
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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/bj/1bjw_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=1bjw ConSurf].
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<div style="clear:both"></div>
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'''ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS'''
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==See Also==
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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== References ==
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==Overview==
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<references/>
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The three-dimensional structures of pyridoxal 5'-phosphate-type aspartate aminotransferase (AspAT) from Thermus thermophilus HB8 and pyridoxamine 5'-phosphate type one in complex with maleate have been determined by X-ray crystallography at 1.8 and 2.6 A resolution, respectively. The enzyme is a homodimer, and the polypeptide chain of the subunit is folded into one arm, one small domain, and one large domain. AspATs from many species were classified into aminotransferase subgroups Ia and Ib. The enzyme belongs to subgroup Ib, its sequence being less than 16% identical to the primary sequences of Escherichia coli, pig cytosolic, and chicken mitochondrial AspATs, which belong to subgroup Ia whose sequences are more than 40% identical and whose three-dimensional structures are quite similar with the active site residues almost completely conserved. The first X-ray analysis of AspAT subgroup Ib indicated that the overall and the active site structures are essentially conserved between the AspATs of subgroup Ia and the enzyme of subgroup Ib, but there are two distinct differences between them. (1) In AspAT subgroup Ia, substrate (or inhibitor) binding induces a large movement of the small domain as a whole to close the active site. However, in the enzyme of subgroup Ib, only the N-terminal region (Lys13-Val30) of the small domain approaches the active site to interact with the maleate. (2) In AspAT subgroup Ia, Arg292 recognizes the side chain carboxylate of the substrate; however, residue 292 of the enzyme in subgroup Ib is not Arg, and in place of Arg292, Lys109 forms a salt bridge with the side chain carboxylate. The thermostability of the enzyme is attained at least in part by the high content of Pro residues in the beta-turns and the marked increase in the number of salt bridges on the molecular surface compared with the mesophilic AspAT.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1BJW is a [[Single protein]] structure of 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=1BJW OCA].
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[[Category: Thermus thermophilus HB8]]
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[[Category: Hirotsu K]]
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==Reference==
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[[Category: Kuramitsu S]]
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Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate., Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K, Biochemistry. 1999 Feb 23;38(8):2413-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10029535 10029535]
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[[Category: Nakai T]]
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[[Category: Aspartate transaminase]]
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[[Category: Okada K]]
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[[Category: Single protein]]
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[[Category: Thermus thermophilus]]
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[[Category: Hirotsu, K.]]
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[[Category: Kuramitsu, S.]]
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[[Category: Nakai, T.]]
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[[Category: Okada, K.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Aminotransferase]]
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[[Category: Pyridoxal enzyme]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:36:41 2008''
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Current revision

ASPARTATE AMINOTRANSFERASE FROM THERMUS THERMOPHILUS

PDB ID 1bjw

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