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1b5o

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{{Seed}}
 
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[[Image:1b5o.png|left|200px]]
 
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==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1==
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The line below this paragraph, containing "STRUCTURE_1b5o", creates the "Structure Box" on the page.
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<StructureSection load='1b5o' size='340' side='right'caption='[[1b5o]], [[Resolution|resolution]] 2.20&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'>[[1b5o]] 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=1B5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5O 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]] 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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_1b5o| PDB=1b5o | 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=1b5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5o OCA], [https://pdbe.org/1b5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5o RCSB], [https://www.ebi.ac.uk/pdbsum/1b5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5o ProSAT]</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/b5/1b5o_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=1b5o 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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Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.
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===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1===
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Substrate recognition mechanism of thermophilic dual-substrate enzyme.,Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S J Biochem. 2001 Jul;130(1):89-98. PMID:11432784<ref>PMID:11432784</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1b5o" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11432784}}, adds the Publication Abstract to the page
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11432784 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11432784}}
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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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1B5O is a 2 chains structure of sequences 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=1B5O 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: Kawaguchi SI]]
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<ref group="xtra">PMID:11432784</ref><references group="xtra"/>
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[[Category: Kuramitsu S]]
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[[Category: Aspartate transaminase]]
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[[Category: Miyahara I]]
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[[Category: Thermus thermophilus]]
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[[Category: Nakai T]]
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[[Category: Hirotsu, K.]]
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[[Category: Ura H]]
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[[Category: Kawaguchi, S I.]]
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[[Category: Kuramitsu, S.]]
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[[Category: Miyahara, I.]]
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[[Category: Nakai, T.]]
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[[Category: Ura, H.]]
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[[Category: Aminotransferase]]
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[[Category: Pyridoxal enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:25:36 2009''
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Current revision

THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE SINGLE MUTANT 1

PDB ID 1b5o

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