6awf

Escherichia coli quinol:fumarate reductase crystallized without dicarboxylate

spinqualitylabelsall models 6awf, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6awf is a 8 chain structure with sequence from Escherichia coli K-12, Escherichia coli O157:H7 and Escherichia coli S88. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.35Å Ligands: F3S, FAD, FES, PO4, SF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. Publication Abstract from PubMed Quinol:fumarate reductase (QFR) is an integral membrane protein and a member of the respiratory Complex II superfamily. Although the structure of Escherichia coli QFR was first reported almost twenty years ago, many open questions of catalysis remain. Here we report two new crystal forms of QFR, one grown from the lipidic cubic phase and one grown from dodecyl maltoside micelles. QFR crystals grown from the lipid cubic phase processed as P1, merged to 7.5A resolution, and exhibited crystal packing similar to previous crystal forms. Crystals grown from dodecyl maltoside micelles processed as P21, merged to 3.35A resolution, and displayed a unique crystal packing. This latter crystal form provides the first view of the E. coli QFR active site without a dicarboxylate ligand. Instead, an unidentified anion binds at a shifted position. In one of the molecules in the asymmetric unit, this is accompanied by rotation of the capping domain of the catalytic subunit. In the other molecule, this is associated with loss of interpretable electron density for this same capping domain. Analysis of the structure suggests that the ligand adjusts the position of the capping domain. New crystal forms of the integral membrane Escherichia coli quinol:fumarate reductase suggest that ligands control domain movement.,Starbird CA, Tomasiak TM, Singh PK, Yankovskaya V, Maklashina E, Eisenbach M, Cecchini G, Iverson TM J Struct Biol. 2017 Nov 20. pii: S1047-8477(17)30193-4. doi:, 10.1016/j.jsb.2017.11.004. PMID:29158068 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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