View source for 5bj3


==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 1==
<StructureSection load='5bj3' size='340' side='right' caption='[[5bj3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5bj3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25104 Atcc 25104]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJ3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5bj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bj3 OCA], [http://pdbe.org/5bj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bj3 RCSB], [http://www.ebi.ac.uk/pdbsum/5bj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bj3 ProSAT]</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/bj/5bj3_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/main_output.php?pdb_ID=5bj3 ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5bj3" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspartate transaminase]]
[[Category: Atcc 25104]]
[[Category: Hirotsu, K]]
[[Category: Kawaguchi, S I]]
[[Category: Kuramitsu, S]]
[[Category: Miyahara, I]]
[[Category: Nakai, T]]
[[Category: Ura, H]]
[[Category: Aminotransferase]]
[[Category: Pyridoxal enzyme]]
[[Category: Transferase]]