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1yoo

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(New page: 200px<br /><applet load="1yoo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yoo, resolution 2.40&Aring;" /> '''ASPARTATE AMINOTRANS...)
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[[Image:1yoo.jpg|left|200px]]<br /><applet load="1yoo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1yoo, resolution 2.40&Aring;" />
 
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'''ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID'''<br />
 
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==Overview==
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==ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID==
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Directed evolution was used to change the substrate specificity of, aspartate aminotransferase. A mutant enzyme with 17 amino acid, substitutions was generated that shows a 2.1 x 10(6)-fold increase in the, catalytic efficiency (kcat/Km) for a non-native substrate, valine. The, absorption spectrum of the bound coenzyme, pyridoxal 5'-phosphate, is also, changed significantly by the mutations. Interestingly, only one of the 17, residues appears to be able to contact the substrate, and none of them, interact with the coenzyme. The three-dimensional structure of the mutant, enzyme complexed with a valine analog, isovalerate (determined to 2.4-A, resolution by x-ray crystallography), provides insights into how the, mutations affect substrate binding. The active site is remodeled; the, subunit interface is altered, and the enzyme domain that encloses the, substrate is shifted by the mutations. The present results demonstrate, clearly the importance of the cumulative effects of residues remote from, the active site and represent a new line of approach to the redesign of, enzyme activity.
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<StructureSection load='1yoo' size='340' side='right'caption='[[1yoo]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yoo]] is a 1 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=1YOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YOO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yoo OCA], [https://pdbe.org/1yoo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yoo RCSB], [https://www.ebi.ac.uk/pdbsum/1yoo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yoo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yo/1yoo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1yoo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Directed evolution was used to change the substrate specificity of aspartate aminotransferase. A mutant enzyme with 17 amino acid substitutions was generated that shows a 2.1 x 10(6)-fold increase in the catalytic efficiency (kcat/Km) for a non-native substrate, valine. The absorption spectrum of the bound coenzyme, pyridoxal 5'-phosphate, is also changed significantly by the mutations. Interestingly, only one of the 17 residues appears to be able to contact the substrate, and none of them interact with the coenzyme. The three-dimensional structure of the mutant enzyme complexed with a valine analog, isovalerate (determined to 2.4-A resolution by x-ray crystallography), provides insights into how the mutations affect substrate binding. The active site is remodeled; the subunit interface is altered, and the enzyme domain that encloses the substrate is shifted by the mutations. The present results demonstrate clearly the importance of the cumulative effects of residues remote from the active site and represent a new line of approach to the redesign of enzyme activity.
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==About this Structure==
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Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.,Oue S, Okamoto A, Yano T, Kagamiyama H J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:9891001<ref>PMID:9891001</ref>
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1YOO 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 PLP and IVA 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=1YOO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biol Chem. 1999 Jan 22;274(4):2344-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9891001 9891001]
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</div>
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[[Category: Aspartate transaminase]]
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<div class="pdbe-citations 1yoo" style="background-color:#fffaf0;"></div>
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Kagamiyama, H.]]
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[[Category: Okamoto, A.]]
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[[Category: Oue, S.]]
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[[Category: Yano, T.]]
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[[Category: IVA]]
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[[Category: PLP]]
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[[Category: aminotransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:57:09 2007''
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==See Also==
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Kagamiyama H]]
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[[Category: Okamoto A]]
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[[Category: Oue S]]
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[[Category: Yano T]]

Current revision

ASPARTATE AMINOTRANSFERASE MUTANT ATB17 WITH ISOVALERIC ACID

PDB ID 1yoo

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