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| | <StructureSection load='1sf2' size='340' side='right'caption='[[1sf2]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1sf2' size='340' side='right'caption='[[1sf2]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sf2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SF2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SF2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sf2]] is a 4 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=1SF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SF2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sff|1sff]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GABT, B2662 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1sf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sf2 OCA], [https://pdbe.org/1sf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sf2 RCSB], [https://www.ebi.ac.uk/pdbsum/1sf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sf2 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-aminobutyrate--2-oxoglutarate_transaminase 4-aminobutyrate--2-oxoglutarate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.19 2.6.1.19] </span></td></tr> | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sf2 OCA], [http://pdbe.org/1sf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sf2 RCSB], [http://www.ebi.ac.uk/pdbsum/1sf2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sf2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GABT_ECOLI GABT_ECOLI]] Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA).<ref>PMID:20639325</ref> | + | [https://www.uniprot.org/uniprot/GABT_ECOLI GABT_ECOLI] Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA).<ref>PMID:20639325</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sf/1sf2_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sf/1sf2_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: 4-aminobutyrate--2-oxoglutarate transaminase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Carter, R J]] | + | [[Category: Carter RJ]] |
| - | [[Category: Fisher, A J]] | + | [[Category: Fisher AJ]] |
| - | [[Category: Langston, J A]] | + | [[Category: Langston JA]] |
| - | [[Category: Liu, W]] | + | [[Category: Liu W]] |
| - | [[Category: Peterson, P E]] | + | [[Category: Peterson PE]] |
| - | [[Category: Toney, M D]] | + | [[Category: Toney MD]] |
| - | [[Category: Zhou, X]] | + | [[Category: Zhou X]] |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GABT_ECOLI Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray crystal structures of Escherichia coli gamma-aminobutyrate aminotransferase unbound and bound to the inhibitor aminooxyacetate are reported. The enzyme crystallizes from ammonium sulfate solutions in the P3(2)21 space group with a tetramer in the asymmetric unit. Diffraction data were collected to 2.4 A resolution for the unliganded enzyme and 1.9 A resolution for the aminooxyacetate complex. The overall structure of the enzyme is similar to those of other aminotransferase subgroup II enzymes. The ability of gamma-aminobutyrate aminotransferase to act on primary amine substrates (gamma-aminobutyrate) in the first half-reaction and alpha-amino acids in the second is proposed to be enabled by the presence of Glu211, whose side chain carboxylate alternates between interactions with Arg398 in the primary amine half-reaction and an alternative binding site in the alpha-amino acid half-reaction, in which Arg398 binds the substrate alpha-carboxylate. The specificity for a carboxylate group on the substrate side chain is due primarily to the presence of Arg141, but also requires substantial local main chain rearrangements relative to the structurally homologous enzyme dialkylglycine decarboxylase, which is specific for small alkyl side chains. No iron-sulfur cluster is found in the bacterial enzyme as was found in the pig enzyme [Storici, P., De Biase, D., Bossa, F., Bruno, S., Mozzarelli, A., Peneff, C., Silverman, R. B., and Schirmer, T. (2004) J. Biol. Chem. 279, 363-73.]. The binding of aminooxyacetate causes remarkably small changes in the active site structure, and no large domain movements are observed. Active site structure comparisons with pig gamma-aminobutyrate aminotransferase and dialkylglycine decarboxylase are discussed.
Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase.,Liu W, Peterson PE, Carter RJ, Zhou X, Langston JA, Fisher AJ, Toney MD Biochemistry. 2004 Aug 31;43(34):10896-905. PMID:15323550[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kurihara S, Kato K, Asada K, Kumagai H, Suzuki H. A putrescine-inducible pathway comprising PuuE-YneI in which gamma-aminobutyrate is degraded into succinate in Escherichia coli K-12. J Bacteriol. 2010 Sep;192(18):4582-91. doi: 10.1128/JB.00308-10. Epub 2010 Jul, 16. PMID:20639325 doi:http://dx.doi.org/10.1128/JB.00308-10
- ↑ Liu W, Peterson PE, Carter RJ, Zhou X, Langston JA, Fisher AJ, Toney MD. Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase. Biochemistry. 2004 Aug 31;43(34):10896-905. PMID:15323550 doi:10.1021/bi049218e
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