1ahf: Difference between revisions
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<StructureSection load='1ahf' size='340' side='right'caption='[[1ahf]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1ahf' size='340' side='right'caption='[[1ahf]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ahf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1ahf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOP:INDOLYLPROPIONIC+ACID'>IOP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOP:INDOLYLPROPIONIC+ACID'>IOP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1ahf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahf OCA], [https://pdbe.org/1ahf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahf RCSB], [https://www.ebi.ac.uk/pdbsum/1ahf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahf ProSAT]</span></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=1ahf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahf OCA], [https://pdbe.org/1ahf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahf RCSB], [https://www.ebi.ac.uk/pdbsum/1ahf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jansonius | [[Category: Jansonius JN]] | ||
[[Category: Malashkevich | [[Category: Malashkevich VN]] | ||
Latest revision as of 08:24, 5 June 2024
ASPARTATE AMINOTRANSFERASE HEXAMUTANTASPARTATE AMINOTRANSFERASE HEXAMUTANT
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMutation of six residues of Escherichia coli aspartate aminotransferase results in substantial acquisition of the transamination properties of tyrosine amino-transferase without loss of aspartate transaminase activity. X-ray crystallographic analysis of key inhibitor complexes of the hexamutant reveals the structural basis for this substrate selectivity. It appears that tyrosine aminotransferase achieves nearly equal affinities for a wide range of amino acids by an unusual conformational switch. An active-site arginine residue either shifts its position to electrostatically interact with charged substrates or moves aside to allow access of aromatic ligands. Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.,Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN Nat Struct Biol. 1995 Jul;2(7):548-53. PMID:7664122[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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