1rhs

SULFUR-SUBSTITUTED RHODANESE

spinqualitylabelsall models 1rhs, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1rhs is a 1 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 1.36Å Ligands: CSS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THTR_BOVIN Together with MRPL18, acts as a mitochondrial import factor for the cytosolic 5S rRNA. Only the nascent unfolded cytoplasmic form is able to bind to the 5S rRNA (By similarity). Formation of iron-sulfur complexes and cyanide detoxification. Binds molecular oxygen and sulfur. 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 1.36 A resolution X-ray diffraction data have been recorded at 100 K for bovine liver sulfur-substituted rhodanese, using synchrotron radiation. The crystal structure has been refined anisotropically to a final R factor of 0.159 (Rfree = 0.229) for 53034 unique reflections. The model contains 2327 protein atoms and 407 solvent molecules, with a good geometry. The high resolution allows full details for helices, beta-sheets, tight turns and of all inter- and intramolecular interactions stabilizing the enzyme molecule to be given. The situation at the active site is described, particularly in regard to the network of hydrogen bonds made by Sgamma and Sdelta of the sulfur-substituted catalytic Cys247 and surrounding groups and solvent molecules. The replacement of the precipitant ammonium sulfate with cryoprotectants in the crystal-suspending medium led to the removal of the sulfate ion from the enzyme active site. Only limited changes of the enzyme structure have been found as a result of the drastic change in the crystal medium. Structure of sulfur-substituted rhodanese at 1.36 A resolution.,Gliubich F, Berni R, Colapietro M, Barba L, Zanotti G Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):481-6. PMID:9761843 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Sulfurtransferase

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