1b5p: Difference between revisions

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{{Seed}}
[[Image:1b5p.png|left|200px]]


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==THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1==
The line below this paragraph, containing "STRUCTURE_1b5p", creates the "Structure Box" on the page.
<StructureSection load='1b5p' size='340' side='right'caption='[[1b5p]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1b5p]] 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=1B5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5P FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
{{STRUCTURE_1b5p|  PDB=1b5p  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5p OCA], [https://pdbe.org/1b5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5p RCSB], [https://www.ebi.ac.uk/pdbsum/1b5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5p ProSAT]</span></td></tr>
</table>
== Function ==
[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>
== 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/b5/1b5p_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=1b5p 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.


===THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE DOUBLE MUTANT 1===
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>
</div>
<div class="pdbe-citations 1b5p" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_11432784}}, adds the Publication Abstract to the page
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 11432784 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_11432784}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1B5P 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=1B5P OCA].
[[Category: Thermus thermophilus HB8]]
 
[[Category: Hirotsu K]]
==Reference==
[[Category: Kawaguchi SI]]
<ref group="xtra">PMID:11432784</ref><references group="xtra"/>
[[Category: Kuramitsu S]]
[[Category: Aspartate transaminase]]
[[Category: Miyahara I]]
[[Category: Thermus thermophilus]]
[[Category: Nakai T]]
[[Category: Hirotsu, K.]]
[[Category: Ura H]]
[[Category: Kawaguchi, S I.]]
[[Category: Kuramitsu, S.]]
[[Category: Miyahara, I.]]
[[Category: Nakai, T.]]
[[Category: Ura, H.]]
[[Category: Aminotransferase]]
[[Category: Pyridoxal enzyme]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 03:58:55 2009''
Retrieved from "https://proteopedia.org/1b5p"