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1cq6

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(New page: 200px<br /><applet load="1cq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cq6, resolution 2.7&Aring;" /> '''ASPARTATE AMINOTRANSF...)
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[[Image:1cq6.jpg|left|200px]]<br /><applet load="1cq6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cq6, resolution 2.7&Aring;" />
 
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'''ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE'''<br />
 
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==Overview==
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==ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE==
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Domain movement is sometimes essential for substrate recognition by an, enzyme. X-ray crystallography of aminotransferase with a series of, aliphatic substrates showed that the domain movement of aspartate, aminotransferase was changed dramatically from an open to a closed form by, the addition of only one CH(2) to the side chain of the C4 substrate, CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results, and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63;, Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364), enabled us to estimate the free energy required for the domain movement.
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<StructureSection load='1cq6' size='340' side='right'caption='[[1cq6]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cq6]] 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=1CQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQ6 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]] 2.7&#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=PY4:2-[O-PHOSPHONOPYRIDOXYL]-AMINO-+BUTYRIC+ACID'>PY4</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=1cq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cq6 OCA], [https://pdbe.org/1cq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cq6 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/cq/1cq6_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=1cq6 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CQ6 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 PY4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1CQ6 OCA].
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*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Free energy requirement for domain movement of an enzyme., Ishijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S, J Biol Chem. 2000 Jun 23;275(25):18939-45. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10858450 10858450]
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[[Category: Aspartate transaminase]]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hirotsu, K.]]
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[[Category: Hirotsu K]]
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[[Category: Ishijima, J.]]
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[[Category: Ishijima J]]
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[[Category: Kawaguchi, S.]]
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[[Category: Kawaguchi S]]
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[[Category: Kuramitsu, S.]]
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[[Category: Kuramitsu S]]
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[[Category: Nakai, T.]]
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[[Category: Nakai T]]
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[[Category: PY4]]
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[[Category: enzyme-substrate complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:40:08 2007''
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Current revision

ASPARTATE AMINOTRANSFERASE COMPLEX WITH C4-PYRIDOXAL-5P-PHOSPHATE

PDB ID 1cq6

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