Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gliubich F, Berni R, Colapietro M, Barba L, Zanotti G. Structure of sulfur-substituted rhodanese at 1.36 A resolution. Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):481-6. PMID:9761843
