6j8m

Low-dose structure of bovine heart cytochrome c oxidase in the fully oxidized state determined using 30 keV X-ray

spinqualitylabelsall models 6j8m, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6j8m is a 20 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CDL, CHD, CU, CUA, DMU, FME, HEA, MG, NA, PEK, PER, PGV, PSC, SAC, TGL, TPO, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COX1_BOVIN Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. Publication Abstract from PubMed To investigate the effect of high-energy X-rays on site-specific radiation-damage, low-dose diffraction data were collected from radiation-sensitive crystals of the metal enzyme cytochrome c oxidase. Data were collected at the Structural Biology I beamline (BL41XU) at SPring-8, using 30 keV X-rays and a highly sensitive pixel array detector equipped with a cadmium telluride sensor. The experimental setup of continuous sample translation using multiple crystals allowed the average diffraction weighted dose per data set to be reduced to 58 kGy, and the resulting data revealed a ligand structure featuring an identical bond length to that in the damage-free structure determined using an X-ray free-electron laser. However, precise analysis of the residual density around the ligand structure refined with the synchrotron data showed the possibility of a small level of specific damage, which might have resulted from the accumulated dose of 58 kGy per data set. Further investigation of the photon-energy dependence of specific damage, as assessed by variations in UV-vis absorption spectra, was conducted using an on-line spectrometer at various energies ranging from 10 to 30 keV. No evidence was found for specific radiation damage being energy dependent. Low-dose X-ray structure analysis of cytochrome c oxidase utilizing high-energy X-rays.,Ueno G, Shimada A, Yamashita E, Hasegawa K, Kumasaka T, Shinzawa-Itoh K, Yoshikawa S, Tsukihara T, Yamamoto M J Synchrotron Radiat. 2019 Jul 1;26(Pt 4):912-921. doi:, 10.1107/S1600577519006805. Epub 2019 Jun 14. PMID:31274413 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c oxidase 3D structures

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