7jz2: Difference between revisions

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'''Unreleased structure'''


The entry 7jz2 is ON HOLD  until Paper Publication
==Succinate: quinone oxidoreductase SQR from E.coli K12==
<StructureSection load='7jz2' size='340' side='right'caption='[[7jz2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jz2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JZ2 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</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=7jz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jz2 OCA], [https://pdbe.org/7jz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jz2 RCSB], [https://www.ebi.ac.uk/pdbsum/7jz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jz2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SDHA_ECOLI SDHA_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.<ref>PMID:24374335</ref> <ref>PMID:12560550</ref> <ref>PMID:16407191</ref> <ref>PMID:19710024</ref>


Authors: Lyu, M., Su, C.-C., Morgan, C.E., Bolla, J.R., Robinson, C.V., Yu, E.W.
==See Also==
 
*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
Description: Succinate: quinone oxidoreductase SQR from E.coli K12
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Bolla, J.R]]
__TOC__
[[Category: Lyu, M]]
</StructureSection>
[[Category: Yu, E.W]]
[[Category: Escherichia coli K-12]]
[[Category: Su, C.-C]]
[[Category: Large Structures]]
[[Category: Morgan, C.E]]
[[Category: Bolla JR]]
[[Category: Robinson, C.V]]
[[Category: Lyu M]]
[[Category: Morgan CE]]
[[Category: Robinson CV]]
[[Category: Su C-C]]
[[Category: Yu EW]]

Latest revision as of 17:54, 6 March 2024

Succinate: quinone oxidoreductase SQR from E.coli K12Succinate: quinone oxidoreductase SQR from E.coli K12

Structural highlights

7jz2 is a 12 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.5Å
Ligands:, , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SDHA_ECOLI Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.[1] [2] [3] [4]

See Also

References

  1. ↑ McNeil MB, Hampton HG, Hards KJ, Watson BN, Cook GM, Fineran PC. The succinate dehydrogenase assembly factor, SdhE, is required for the flavinylation and activation of fumarate reductase in bacteria. FEBS Lett. 2014 Jan 31;588(3):414-21. doi: 10.1016/j.febslet.2013.12.019. Epub, 2013 Dec 25. PMID:24374335 doi:http://dx.doi.org/10.1016/j.febslet.2013.12.019
  2. ↑ Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S. Architecture of succinate dehydrogenase and reactive oxygen species generation. Science. 2003 Jan 31;299(5607):700-4. PMID:12560550 doi:10.1126/science.1079605
  3. ↑ Horsefield R, Yankovskaya V, Sexton G, Whittingham W, Shiomi K, Omura S, Byrne B, Cecchini G, Iwata S. Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction. J Biol Chem. 2006 Mar 17;281(11):7309-16. Epub 2005 Dec 27. PMID:16407191 doi:http://dx.doi.org/10.1074/jbc.M508173200
  4. ↑ Ruprecht J, Yankovskaya V, Maklashina E, Iwata S, Cecchini G. Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site. J Biol Chem. 2009 Oct 23;284(43):29836-46. Epub 2009 Aug 25. PMID:19710024 doi:10.1074/jbc.M109.010058

7jz2, resolution 2.50Å

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