4d7e: Difference between revisions
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==An unprecedented NADPH domain conformation in Lysine Monooxygenase NbtG from Nocardia farcinica== | ==An unprecedented NADPH domain conformation in Lysine Monooxygenase NbtG from Nocardia farcinica== | ||
<StructureSection load='4d7e' size='340' side='right' caption='[[4d7e]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4d7e' size='340' side='right' caption='[[4d7e]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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<table><tr><td colspan='2'>[[4d7e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D7E FirstGlance]. <br> | <table><tr><td colspan='2'>[[4d7e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D7E FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4d7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d7e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d7e RCSB], [http://www.ebi.ac.uk/pdbsum/4d7e PDBsum]</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=4d7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d7e OCA], [http://pdbe.org/4d7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d7e RCSB], [http://www.ebi.ac.uk/pdbsum/4d7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d7e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4d7e" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 20:36, 9 March 2017
An unprecedented NADPH domain conformation in Lysine Monooxygenase NbtG from Nocardia farcinicaAn unprecedented NADPH domain conformation in Lysine Monooxygenase NbtG from Nocardia farcinica
Structural highlights
Publication Abstract from PubMedN-hydroxylating monooxygenases (NMOs) are involved in the biosynthesis of iron-chelating hydroxamate-containing siderophores that play a role in microbial virulence. These flavoenzymes catalyze the NADPH- and oxygen-dependent hydroxylation of amines, such as those found on the side chains of lysine and ornithine. In this work we report the biochemical and structural characterization of Nocardia farcinica Lys-monooxygenase (NbtG), which has similar biochemical properties to mycobacterial homologs. NbtG is also active on D-Lys although it binds L-Lys with a higher affinity. Differently from the ornithine monooxygenases PvdA, SidA and KtzI, NbtG can use both NADH and NADPH and is highly uncoupled, producing more superoxide and hydrogen peroxide than hydroxylated Lys. The crystal structure of NbtG solved at 2.4 A resolution revealed an unexpected protein conformation with a 30 degrees rotation of the NAD(P)H domain with respect to the FAD domain that precludes binding of the nicotinamide cofactor. This occluded structure may explain the biochemical properties of NbtG, specifically with regard to the substantial uncoupling and limited stabilization of the C4a-hydroperoxyflavin intermediate. Biological implications of these findings are discussed. An Unprecedented NADPH Domain Conformation in Lysine Monooxygenase NbtG Provides Insights Into Uncoupling of Oxygen Consumption From Substrate Hydroxylation.,Binda C, Robinson RM, Martin Del Campo JS, Keul ND, Rodriguez PJ, Robinson HH, Mattevi A, Sobrado P J Biol Chem. 2015 Mar 23. pii: jbc.M114.629485. PMID:25802330[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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