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| <StructureSection load='4atp' size='340' side='right'caption='[[4atp]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4atp' size='340' side='right'caption='[[4atp]], [[Resolution|resolution]] 2.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4atp]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_aurescens_tc1 Arthrobacter aurescens tc1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ATP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4atp]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenarthrobacter_aurescens_TC1 Paenarthrobacter aurescens TC1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ATP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ATP FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 2.8Å</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='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> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4atp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atp OCA], [http://pdbe.org/4atp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4atp RCSB], [http://www.ebi.ac.uk/pdbsum/4atp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4atp ProSAT]</span></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=4atp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4atp OCA], [https://pdbe.org/4atp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4atp RCSB], [https://www.ebi.ac.uk/pdbsum/4atp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4atp ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/A1R958_PAEAT A1R958_PAEAT] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: 4-aminobutyrate--2-oxoglutarate transaminase]] | + | [[Category: Large Structures]] |
- | [[Category: Arthrobacter aurescens tc1]] | + | [[Category: Paenarthrobacter aurescens TC1]] |
- | [[Category: Bruce, H]] | + | [[Category: Bruce H]] |
- | [[Category: Grogan, G]] | + | [[Category: Grogan G]] |
- | [[Category: Hart, S]] | + | [[Category: Hart S]] |
- | [[Category: Sanchez, J Mangas]] | + | [[Category: Mangas Sanchez J]] |
- | [[Category: Tuan, A N]] | + | [[Category: Tuan AN]] |
- | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
- | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A1R958_PAEAT
Publication Abstract from PubMed
Two complex structures of the gamma-aminobutyrate (GABA) transaminase A1R958 from Arthrobacter aurescens TC1 are presented. The first, determined to a resolution of 2.80 A, features the internal aldimine formed by reaction between the -amino group of Lys295 and the cofactor pyridoxal phosphate (PLP); the second, determined to a resolution of 2.75 A, features the external aldimine adduct formed between PLP and GABA in the first half-reaction. This is the first structure of a microbial GABA transaminase in complex with its natural external aldimine and reveals the molecular determinants of GABA binding in this enzyme.
Structures of a gamma-aminobutyrate (GABA) transaminase from the s-triazine-degrading organism Arthrobacter aurescens TC1 in complex with PLP and with its external aldimine PLP-GABA adduct.,Bruce H, Nguyen Tuan A, Mangas Sanchez J, Leese C, Hopwood J, Hyde R, Hart S, Turkenburg JP, Grogan G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1175-80., doi: 10.1107/S1744309112030023. Epub 2012 Sep 29. PMID:23027742[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bruce H, Nguyen Tuan A, Mangas Sanchez J, Leese C, Hopwood J, Hyde R, Hart S, Turkenburg JP, Grogan G. Structures of a gamma-aminobutyrate (GABA) transaminase from the s-triazine-degrading organism Arthrobacter aurescens TC1 in complex with PLP and with its external aldimine PLP-GABA adduct. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1175-80., doi: 10.1107/S1744309112030023. Epub 2012 Sep 29. PMID:23027742 doi:http://dx.doi.org/10.1107/S1744309112030023
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