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| | <StructureSection load='4b9b' size='340' side='right'caption='[[4b9b]], [[Resolution|resolution]] 1.64Å' scene=''> | | <StructureSection load='4b9b' size='340' side='right'caption='[[4b9b]], [[Resolution|resolution]] 1.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b9b]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B9B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b9b]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B9B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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]] 1.64Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b98|4b98]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-alanine--pyruvate_transaminase Beta-alanine--pyruvate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.18 2.6.1.18] </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=4b9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9b OCA], [https://pdbe.org/4b9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b9b RCSB], [https://www.ebi.ac.uk/pdbsum/4b9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9b 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=4b9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b9b OCA], [https://pdbe.org/4b9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b9b RCSB], [https://www.ebi.ac.uk/pdbsum/4b9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b9b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BAUA_PSEAE BAUA_PSEAE] Involved in the degradation of beta-alanine. Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L-alanine and 3-oxopropanoate. It can also accept both 4-aminobutyrate and (S)-alpha-methylbenzylamine (MBA) as amino-group donors in the presence of pyruvate as an amine acceptor.<ref>PMID:21622750</ref> <ref>PMID:23519665</ref> |
| | <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: Beta-alanine--pyruvate transaminase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Isupov, M N]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Littlechild, J A]] | + | [[Category: Isupov MN]] |
| - | [[Category: Sayer, C]] | + | [[Category: Littlechild JA]] |
| - | [[Category: Westlake, A]] | + | [[Category: Sayer C]] |
| - | [[Category: Transferase]] | + | [[Category: Westlake A]] |
| Structural highlights
Function
BAUA_PSEAE Involved in the degradation of beta-alanine. Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L-alanine and 3-oxopropanoate. It can also accept both 4-aminobutyrate and (S)-alpha-methylbenzylamine (MBA) as amino-group donors in the presence of pyruvate as an amine acceptor.[1] [2]
Publication Abstract from PubMed
The crystal structures and inhibitor complexes of two industrially important omega-aminotransferase enzymes from Pseudomonas aeruginosa and Chromobacterium violaceum have been determined in order to understand the differences in their substrate specificity. The two enzymes share 30% sequence identity and use the same amino acceptor, pyruvate; however, the Pseudomonas enzyme shows activity towards the amino donor beta-alanine, whilst the Chromobacterium enzyme does not. Both enzymes show activity towards S-alpha-methylbenzylamine (MBA), with the Chromobacterium enzyme having a broader substrate range. The crystal structure of the P. aeruginosa enzyme has been solved in the holo form and with the inhibitor gabaculine bound. The C. violaceum enzyme has been solved in the apo and holo forms and with gabaculine bound. The structures of the holo forms of both enzymes are quite similar. There is little conformational difference observed between the inhibitor complex and the holoenzyme for the P. aeruginosa aminotransferase. In comparison, the crystal structure of the C. violaceum gabaculine complex shows significant structural rearrangements from the structures of both the apo and holo forms of the enzyme. It appears that the different rigidity of the protein scaffold contributes to the substrate specificity observed for the two omega-aminotransferases.
Structural studies of Pseudomonas and Chromobacterium omega-aminotransferases provide insights into their differing substrate specificity.,Sayer C, Isupov MN, Westlake A, Littlechild JA Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):564-76. doi:, 10.1107/S0907444912051670. Epub 2013 Mar 14. PMID:23519665[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yao X, He W, Lu CD. Functional characterization of seven γ-Glutamylpolyamine synthetase genes and the bauRABCD locus for polyamine and β-Alanine utilization in Pseudomonas aeruginosa PAO1. J Bacteriol. 2011 Aug;193(15):3923-30. PMID:21622750 doi:10.1128/JB.05105-11
- ↑ Sayer C, Isupov MN, Westlake A, Littlechild JA. Structural studies of Pseudomonas and Chromobacterium omega-aminotransferases provide insights into their differing substrate specificity. Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):564-76. doi:, 10.1107/S0907444912051670. Epub 2013 Mar 14. PMID:23519665 doi:10.1107/S0907444912051670
- ↑ Sayer C, Isupov MN, Westlake A, Littlechild JA. Structural studies of Pseudomonas and Chromobacterium omega-aminotransferases provide insights into their differing substrate specificity. Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):564-76. doi:, 10.1107/S0907444912051670. Epub 2013 Mar 14. PMID:23519665 doi:10.1107/S0907444912051670
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