6lum

<table><tr><td colspan='2'>[[6lum]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_mc2_51 Mycolicibacterium smegmatis mc2 51]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LUM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LUM FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+HEXADECANOATE'>LPP</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene>, <scene name='pdbligand=PEV:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PEV</scene>, <scene name='pdbligand=PIE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOINOSITOL'>PIE</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lum OCA], [http://pdbe.org/6lum PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lum RCSB], [http://www.ebi.ac.uk/pdbsum/6lum PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lum ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Diheme-containing succinate:menaquinone oxidoreductases (Sdh) are widespread in Gram-positive bacteria but little is known about the catalytic mechanisms they employ for succinate oxidation by menaquinone. Here, we present the 2.8 A cryo-electron microscopy structure of a Mycobacterium smegmatis Sdh, which forms a trimer. We identified the membrane-anchored SdhF as a subunit of the complex. The 3 kDa SdhF forms a single transmembrane helix and this helix plays a role in blocking the canonically proximal quinone-binding site. We also identified two distal quinone-binding sites with bound quinones. One distal binding site is formed by neighboring subunits of the complex. Our structure further reveals the electron/proton transfer pathway for succinate oxidation by menaquinone. Moreover, this study provides further structural insights into the physiological significance of a trimeric respiratory complex II. The structure of the menaquinone binding site could provide a framework for the development of Sdh-selective anti-mycobacterial drugs.

 

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== References ==

[[Category: Gao, Y]]

[[Category: Gong, H]]

[[Category: Ji, W]]

[[Category: Rao, Z]]

[[Category: Wang, Q]]

[[Category: Wang, W]]

[[Category: Xiao, Y]]

[[Category: Zhou, X]]

[[Category: Trimer]]