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1a3g

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[[Image:1a3g.gif|left|200px]]
 
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{{Structure
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==BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI==
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|PDB= 1a3g |SIZE=350|CAPTION= <scene name='initialview01'>1a3g</scene>, resolution 2.5&Aring;
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<StructureSection load='1a3g' size='340' side='right'caption='[[1a3g]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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<table><tr><td colspan='2'>[[1a3g]] is a 3 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=1A3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A3G FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42]
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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]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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}}
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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=1a3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a3g OCA], [https://pdbe.org/1a3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a3g RCSB], [https://www.ebi.ac.uk/pdbsum/1a3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a3g ProSAT]</span></td></tr>
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</table>
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'''BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI'''
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== Function ==
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[https://www.uniprot.org/uniprot/ILVE_ECOLI ILVE_ECOLI] Acts on leucine, isoleucine and valine.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The X-ray crystallographic structure of the branched-chain amino acid aminotransferase from Escherichia coli was determined by means of isomorphous replacement using the selenomethionyl enzyme as one of the heavy atom derivatives. The enzyme is a homo hexamer with D3 symmetry, and the polypeptide chain of the subunit is folded into two domains (small and large domains). The coenzyme, pyridoxal 5'-phosphate, resides at the domain interface, its re-face facing toward the protein. The active site structure shows that the following sites can recognize branched-chain amino acids and glutamate as substrates: (1) a hydrophobic core formed by Phe36, Tyr164, Tyr31*, and Val109* for a branched-chain; (2) Arg97 for an acidic side chain of glutamate; and (3) Tyr95 and two main chain NH groups of Thr257 and Ala258 for the alpha-carboxylate of substrates. Although the main chain conformation of the active site is homologous to that of D-amino acid aminotransferase, many of the active site residues are different between them.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a3/1a3g_consurf.spt"</scriptWhenChecked>
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1A3G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A3G OCA].
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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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==Reference==
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</jmolCheckbox>
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Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution., Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H, J Biochem. 1997 Apr;121(4):637-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9163511 9163511]
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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=1a3g ConSurf].
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[[Category: Branched-chain-amino-acid transaminase]]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[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: Hayashi, H.]]
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[[Category: Hayashi H]]
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[[Category: Hirotsu, K.]]
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[[Category: Hirotsu K]]
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[[Category: Kagamiyama, H.]]
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[[Category: Kagamiyama H]]
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[[Category: Okada, K.]]
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[[Category: Okada K]]
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[[Category: Sato, M.]]
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[[Category: Sato M]]
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[[Category: PLP]]
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[[Category: aminotransferase]]
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[[Category: pyridoxal enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:03:59 2008''
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Current revision

BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI

PDB ID 1a3g

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