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==Structural and functional study of succinyl-ornithine transaminase from E. coli== | |||
<StructureSection load='4add' size='340' side='right' caption='[[4add]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4add]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ADD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ADD 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>, <scene name='pdbligand=SUO:N~2~-(3-CARBOXYPROPANOYL)-L-ORNITHINE'>SUO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4adb|4adb]], [[4ade|4ade]], [[4adc|4adc]]</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=4add FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4add OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4add RCSB], [http://www.ebi.ac.uk/pdbsum/4add PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
possesses two acyl ornithine aminotransferases, one catabolic (AstC) and the other anabolic (ArgD), that participate in L-arginine metabolism. Although only 58% identical, the enzymes have been shown to be functionally interchangeable. Here we have purified AstC and have obtained X-ray crystal structures of apo and holo-AstC and of the enzyme complexed with its physiological substrate, succinylornithine. We compare the structures obtained in this study with those of ArgD from obtained elsewhere, finding several notable differences. Docking studies were used to explore the docking modes of several substrates (ornithine, succinylornithine and acetylornithine) and the co-substrate glutamate/alpha-ketogluterate. The docking studies support our observations that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme. | |||
Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (AstC) from Escherichia coli.,Newman J, Seabrook S, Surjadi R, Williams CC, Lucent D, Wilding M, Scott C, Peat TS PLoS One. 2013;8(3):e58298. doi: 10.1371/journal.pone.0058298. Epub 2013 Mar 6. PMID:23484010<ref>PMID:23484010</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
<references | __TOC__ | ||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Newman, J | [[Category: Newman, J]] | ||
[[Category: Peat, T S | [[Category: Peat, T S]] | ||
[[Category: Aminotransferase]] | [[Category: Aminotransferase]] | ||
[[Category: Plp enzyme]] | [[Category: Plp enzyme]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 13:02, 21 December 2014
Structural and functional study of succinyl-ornithine transaminase from E. coliStructural and functional study of succinyl-ornithine transaminase from E. coli
Structural highlights
Publication Abstract from PubMedpossesses two acyl ornithine aminotransferases, one catabolic (AstC) and the other anabolic (ArgD), that participate in L-arginine metabolism. Although only 58% identical, the enzymes have been shown to be functionally interchangeable. Here we have purified AstC and have obtained X-ray crystal structures of apo and holo-AstC and of the enzyme complexed with its physiological substrate, succinylornithine. We compare the structures obtained in this study with those of ArgD from obtained elsewhere, finding several notable differences. Docking studies were used to explore the docking modes of several substrates (ornithine, succinylornithine and acetylornithine) and the co-substrate glutamate/alpha-ketogluterate. The docking studies support our observations that AstC has a strong preference for acylated ornithine species over ornithine itself, and suggest that the increase in specificity associated with acylation is caused by steric and desolvation effects rather than specific interactions between the substrate and enzyme. Determination of the Structure of the Catabolic N-Succinylornithine Transaminase (AstC) from Escherichia coli.,Newman J, Seabrook S, Surjadi R, Williams CC, Lucent D, Wilding M, Scott C, Peat TS PLoS One. 2013;8(3):e58298. doi: 10.1371/journal.pone.0058298. Epub 2013 Mar 6. PMID:23484010[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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