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4kx6
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4kx6 is ON HOLD Authors: Singh, P.K., Sarwar, M., Maklashina, E., Kotlyar, V., Rajagukguk, S., Tomasiak, T.M., Cecchini, G., Iverson, T.M. Descript...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Plasticity of the quinone-binding site of the complex II homolog quinol:fumarate reductase== | |
| - | + | <StructureSection load='4kx6' size='340' side='right'caption='[[4kx6]], [[Resolution|resolution]] 2.95Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4kx6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BW2952 Escherichia coli BW2952], [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1] and [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=4KX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KX6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</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=MQ7:MENAQUINONE-7'>MQ7</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=4kx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kx6 OCA], [https://pdbe.org/4kx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kx6 RCSB], [https://www.ebi.ac.uk/pdbsum/4kx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kx6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FRDA_ECOLI FRDA_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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli BW2952]] | ||
| + | [[Category: Escherichia coli DH1]] | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cecchini G]] | ||
| + | [[Category: Iverson TM]] | ||
| + | [[Category: Kotlyar V]] | ||
| + | [[Category: Maklashina E]] | ||
| + | [[Category: Rajagukguk S]] | ||
| + | [[Category: Sarwar M]] | ||
| + | [[Category: Singh PK]] | ||
| + | [[Category: Tomasiak TM]] | ||
Current revision
Plasticity of the quinone-binding site of the complex II homolog quinol:fumarate reductase
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