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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4BA4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4ba4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ba4 OCA], [https://pdbe.org/4ba4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ba4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ba4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ba4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q7NWG4_CHRVO Q7NWG4_CHRVO] | |||
<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> | |||
<div class="pdbe-citations 4ba4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chromobacterium violaceum]] | |||
[[Category: Large Structures]] | |||
[[Category: Isupov MN]] | |||
[[Category: Littlechild JA]] | |||
[[Category: Sayer C]] | |||
Latest revision as of 14:46, 20 December 2023
Crystal structure of the apo omega-transaminase from Chromobacterium violaceumCrystal structure of the apo omega-transaminase from Chromobacterium violaceum
Structural highlights
FunctionPublication 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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