5bj3
From Proteopedia
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| - | [[ | + | ==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 1== |
| + | <StructureSection load='5bj3' size='340' side='right' caption='[[5bj3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5bj3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. 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://www.rcsb.org/pdb/explore.do?structureId=5bj3 RCSB], [http://www.ebi.ac.uk/pdbsum/5bj3 PDBsum]</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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Aspartate Aminotransferase|Aspartate Aminotransferase]] | *[[Aspartate Aminotransferase|Aspartate Aminotransferase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
| - | [[Category: Hirotsu, K | + | [[Category: Hirotsu, K]] |
| - | [[Category: Kawaguchi, S I | + | [[Category: Kawaguchi, S I]] |
| - | [[Category: Kuramitsu, S | + | [[Category: Kuramitsu, S]] |
| - | [[Category: Miyahara, I | + | [[Category: Miyahara, I]] |
| - | [[Category: Nakai, T | + | [[Category: Nakai, T]] |
| - | [[Category: Ura, H | + | [[Category: Ura, H]] |
[[Category: Aminotransferase]] | [[Category: Aminotransferase]] | ||
[[Category: Pyridoxal enzyme]] | [[Category: Pyridoxal enzyme]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 16:52, 10 December 2014
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 1
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