5kmp: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
The | ==The structure of G164E variant of type II NADH dehydrogenase from Caldalkalibacillus thermarum== | ||
<StructureSection load='5kmp' size='340' side='right' caption='[[5kmp]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5kmp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KMP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KMP 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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kmq|5kmq]], [[5kmr|5kmr]], [[5kms|5kms]]</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=5kmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kmp OCA], [http://pdbe.org/5kmp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kmp RCSB], [http://www.ebi.ac.uk/pdbsum/5kmp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kmp ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Type II NADH:quinone oxidoreductase (NDH-2) is central to the respiratory chains of many organisms. It is not present in mammals so may be exploited as an antimicrobial drug target or used as a substitute for dysfunctional respiratory complex I in neuromuscular disorders. NDH-2 is a single-subunit monotopic membrane protein with just a flavin cofactor, yet no consensus exists on its mechanism. Here, we use steady-state and pre-steady-state kinetics combined with mutagenesis and structural studies to determine the mechanism of NDH-2 from Caldalkalibacillus thermarum. We show that the two substrate reactions occur independently, at different sites, and regardless of the occupancy of the partner site. We conclude that the reaction pathway is determined stochastically, by the substrate/product concentrations and dissociation constants, and can follow either a ping-pong or ternary mechanism. This mechanistic versatility provides a unified explanation for all extant data and a new foundation for the development of therapeutic strategies. | |||
The mechanism of catalysis by type-II NADH:quinone oxidoreductases.,Blaza JN, Bridges HR, Aragao D, Dunn EA, Heikal A, Cook GM, Nakatani Y, Hirst J Sci Rep. 2017 Jan 9;7:40165. doi: 10.1038/srep40165. PMID:28067272<ref>PMID:28067272</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5kmp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aragao, D]] | [[Category: Aragao, D]] | ||
[[Category: Cook, G M]] | |||
[[Category: Nakatani, Y]] | [[Category: Nakatani, Y]] | ||
[[Category: | [[Category: Nadh dehydrogenase]] | ||
[[Category: Oxidoreductase]] | |||
[[Category: Rossmann fold]] | |||
Revision as of 23:28, 25 January 2017
The structure of G164E variant of type II NADH dehydrogenase from Caldalkalibacillus thermarum
| ||||||||||||
