4ba4: Difference between revisions
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==Crystal structure of the apo omega-transaminase from Chromobacterium violaceum== | |||
<StructureSection load='4ba4' size='340' side='right' caption='[[4ba4]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ba4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chromobacterium_violaceum Chromobacterium violaceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BA4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4a6r|4a6r]], [[4a6t|4a6t]], [[4a6u|4a6u]], [[4a72|4a72]], [[4ah3|4ah3]], [[4ba5|4ba5]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-alanine--pyruvate_transaminase Beta-alanine--pyruvate transaminase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ba4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ba4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ba4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ba4 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23519665</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Beta-alanine--pyruvate transaminase]] | [[Category: Beta-alanine--pyruvate transaminase]] | ||
[[Category: Chromobacterium violaceum]] | [[Category: Chromobacterium violaceum]] | ||
[[Category: Isupov, M N | [[Category: Isupov, M N]] | ||
[[Category: Littlechild, J A | [[Category: Littlechild, J A]] | ||
[[Category: Sayer, C | [[Category: Sayer, C]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 16:08, 4 January 2015
Crystal structure of the apo omega-transaminase from Chromobacterium violaceumCrystal structure of the apo omega-transaminase from Chromobacterium violaceum
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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