1ahf: Difference between revisions

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-[[Image:1ahf.gif|left|200px]]<br /><applet load="1ahf" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ahf, resolution 2.3&Aring;" />
-'''ASPARTATE AMINOTRANSFERASE HEXAMUTANT'''<br />
-==Overview==
+==ASPARTATE AMINOTRANSFERASE HEXAMUTANT==
-Mutation 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.
+<StructureSection load='1ahf' size='340' side='right'caption='[[1ahf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
+== 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/ah/1ahf_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=1ahf ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Mutation 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.
-==About this Structure==
+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<ref>PMID:7664122</ref>
-AHF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4, PLP and IOP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AHF OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7664122 7664122]
+</div>
-[[Category: Aspartate transaminase]]
+<div class="pdbe-citations 1ahf" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Jansonius, J.N.]]
+[[Category: Jansonius JN]]
-[[Category: Malashkevich, V.N.]]
+[[Category: Malashkevich VN]]
-[[Category: IOP]]
-[[Category: PLP]]
-[[Category: SO4]]
-[[Category: transferase (aminotransferase)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:51:24 2007''