1utg

REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1utg, resolution 1.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1utg is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.34Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UTER_RABIT Uteroglobin binds progesterone specifically and with high affinity. It may regulate progesterone concentrations reaching the blastocyst. It is also a potent inhibitor of phospholipase A2. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of uteroglobin, a progesterone binding protein from rabbit uterine fluid, was determined and refined at 1.34 A resolution to a conventional R-factor of 0.229. The accuracy of the co-ordinates is estimated to be 0.15 A. The isotropic temperature factor of individual atoms was refined and its average value is 11.9 A2 for the 548 non-hydrogen atoms of the protein monomer. A total of 83 water molecules was located in difference electron density maps and refined, first using a constant occupancy factor of 1 and then variable occupancy, the final (Q) being 0.63. The mean temperature factor of the water oxygen atoms is 26.4 A2. Uteroglobin is a dimer and its secondary structure consists of four alpha-helices per monomer that align in an anti-parallel fashion. There is one beta-turn between helix 2 and helix 3 (Lys26 to Glu29); 76% of the residues are part of the alpha-helices. In the core of the dimeric protein molecule, between the two monomers that are held together by two disulfide bridges, we have observed a closed cavity. Its length is 15.6 A and its width is 9 A; 14 water molecules could be positioned inside. In the "bottom" part of the protein, near the C terminus, we have observed a smaller cavity, occupied by two water molecules. The calculation of the molecular surface revealed four surface pockets whose possible functional implications are discussed below. Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution.,Morize I, Surcouf E, Vaney MC, Epelboin Y, Buehner M, Fridlansky F, Milgrom E, Mornon JP J Mol Biol. 1987 Apr 20;194(4):725-39. PMID:3656405 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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