7d6x: Difference between revisions
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==Mycobacterium smegmatis Sdh1 complex in the apo form== | |||
<StructureSection load='7d6x' size='340' side='right'caption='[[7d6x]], [[Resolution|resolution]] 2.88Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7d6x]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D6X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D6X FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.88Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=PEV:(1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL+STEARATE'>PEV</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'>[https://proteopedia.org/fgij/fg.htm?mol=7d6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d6x OCA], [https://pdbe.org/7d6x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d6x RCSB], [https://www.ebi.ac.uk/pdbsum/7d6x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d6x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0QPJ3_MYCS2 A0QPJ3_MYCS2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Complex II, also known as succinate dehydrogenase (SQR) or fumarate reductase (QFR), is an enzyme involved in both the Krebs cycle and oxidative phosphorylation. Mycobacterial Sdh1 has recently been identified as a new class of respiratory complex II (type F) but with an unknown electron transfer mechanism. Here, using cryoelectron microscopy, we have determined the structure of Mycobacterium smegmatis Sdh1 in the presence and absence of the substrate, ubiquinone-1, at 2.53-A and 2.88-A resolution, respectively. Sdh1 comprises three subunits, two that are water soluble, SdhA and SdhB, and one that is membrane spanning, SdhC. Within these subunits we identified a quinone-binding site and a rarely observed Rieske-type [2Fe-2S] cluster, the latter being embedded in the transmembrane region. A mutant, where two His ligands of the Rieske-type [2Fe-2S] were changed to alanine, abolished the quinone reduction activity of the Sdh1. Our structures allow the proposal of an electron transfer pathway that connects the substrate-binding and quinone-binding sites. Given the unique features of Sdh1 and its essential role in Mycobacteria, these structures will facilitate antituberculosis drug discovery efforts that specifically target this complex. | |||
Architecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster.,Zhou X, Gao Y, Wang W, Yang X, Yang X, Liu F, Tang Y, Lam SM, Shui G, Yu L, Tian C, Guddat LW, Wang Q, Rao Z, Gong H Proc Natl Acad Sci U S A. 2021 Apr 13;118(15):e2022308118. doi: , 10.1073/pnas.2022308118. PMID:33876763<ref>PMID:33876763</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7d6x" style="background-color:#fffaf0;"></div> | ||
[[Category: Gao | |||
[[Category: | ==See Also== | ||
[[Category: Wang | *[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycolicibacterium smegmatis]] | |||
[[Category: Gao Y]] | |||
[[Category: Gong H]] | |||
[[Category: Rao Z]] | |||
[[Category: Wang Q]] | |||
[[Category: Zhou X]] | |||
Latest revision as of 22:31, 29 May 2024
Mycobacterium smegmatis Sdh1 complex in the apo formMycobacterium smegmatis Sdh1 complex in the apo form
Structural highlights
FunctionPublication Abstract from PubMedComplex II, also known as succinate dehydrogenase (SQR) or fumarate reductase (QFR), is an enzyme involved in both the Krebs cycle and oxidative phosphorylation. Mycobacterial Sdh1 has recently been identified as a new class of respiratory complex II (type F) but with an unknown electron transfer mechanism. Here, using cryoelectron microscopy, we have determined the structure of Mycobacterium smegmatis Sdh1 in the presence and absence of the substrate, ubiquinone-1, at 2.53-A and 2.88-A resolution, respectively. Sdh1 comprises three subunits, two that are water soluble, SdhA and SdhB, and one that is membrane spanning, SdhC. Within these subunits we identified a quinone-binding site and a rarely observed Rieske-type [2Fe-2S] cluster, the latter being embedded in the transmembrane region. A mutant, where two His ligands of the Rieske-type [2Fe-2S] were changed to alanine, abolished the quinone reduction activity of the Sdh1. Our structures allow the proposal of an electron transfer pathway that connects the substrate-binding and quinone-binding sites. Given the unique features of Sdh1 and its essential role in Mycobacteria, these structures will facilitate antituberculosis drug discovery efforts that specifically target this complex. Architecture of the mycobacterial succinate dehydrogenase with a membrane-embedded Rieske FeS cluster.,Zhou X, Gao Y, Wang W, Yang X, Yang X, Liu F, Tang Y, Lam SM, Shui G, Yu L, Tian C, Guddat LW, Wang Q, Rao Z, Gong H Proc Natl Acad Sci U S A. 2021 Apr 13;118(15):e2022308118. doi: , 10.1073/pnas.2022308118. PMID:33876763[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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