4f5f: Difference between revisions
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==Structure of Aspartate Aminotransferase Conversion to Tyrosine Aminotransferase: Chimera P1.== | ==Structure of Aspartate Aminotransferase Conversion to Tyrosine Aminotransferase: Chimera P1.== | ||
<StructureSection load='4f5f' size='340' side='right' caption='[[4f5f]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='4f5f' size='340' side='right'caption='[[4f5f]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4f5f]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4f5f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F5F FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><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></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f5f OCA], [https://pdbe.org/4f5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f5f RCSB], [https://www.ebi.ac.uk/pdbsum/4f5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f5f ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Aspartate | *[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Addington | [[Category: Addington TA]] | ||
[[Category: Fisher | [[Category: Fisher AJ]] | ||
[[Category: Toney | [[Category: Toney MD]] | ||
Latest revision as of 07:36, 7 October 2022
Structure of Aspartate Aminotransferase Conversion to Tyrosine Aminotransferase: Chimera P1.Structure of Aspartate Aminotransferase Conversion to Tyrosine Aminotransferase: Chimera P1.
Structural highlights
FunctionPublication Abstract from PubMedIdentification of residues responsible for functional specificity in enzymes is a challenging and important problem in protein chemistry. Active-site residues are generally easy to identify, but residues outside the active site are also important to catalysis and their identities and roles are more difficult to determine. We report a method based on analysis of multiple sequence alignments, embodied in our program Janus, for predicting mutations required to interconvert structurally related but functionally distinct enzymes. Conversion of aspartate aminotransferase into tyrosine aminotransferase is demonstrated and compared to previous efforts. Incorporation of 35 predicted mutations resulted in an enzyme with the desired substrate specificity but low catalytic activity. A single round of DNA back-shuffling with wild-type aspartate aminotransferase on this variant generated mutants with tyrosine aminotransferase activities better than those previously realized from rational design or directed evolution. Methods such as this, coupled with computational modeling, may prove invaluable in furthering our understanding of enzyme catalysis and engineering. Janus: Prediction and Ranking of Mutations Required for Functional Interconversion of Enzymes.,Addington TA, Mertz RW, Siegel JB, Thompson JM, Fisher AJ, Filkov V, Fleischman N, Suen A, Zhang C, Toney MD J Mol Biol. 2013 Feb 6. pii: S0022-2836(13)00065-X. doi:, 10.1016/j.jmb.2013.01.034. PMID:23396064[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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