1RHS

SULFUR-SUBSTITUTED RHODANESE

Summary for 1RHS

• Entry DOI: 10.2210/pdb1rhs/pdb
• Descriptor: SULFUR-SUBSTITUTED RHODANESE (2 entities in total)
• Functional Keywords: transferase, rhodanese, sulfurtransferase
• Biological source: Bos taurus (cattle)
• Cellular location: Mitochondrion matrix: P00586
• Total number of polymer chains: 1
• Total formula weight: 33240.67

Authors

Zanotti, G.,Gliubich, F.,Colapietro, M.,Barba, L. (deposition date: 1997-07-16, release date: 1998-01-21, Last modification date: 2024-10-30)

Primary citation

Gliubich, F.,Berni, R.,Colapietro, M.,Barba, L.,Zanotti, G.
Structure of sulfur-substituted rhodanese at 1.36 A resolution.
Acta Crystallogr.,Sect.D, 54:481-486, 1998

PubMed Abstract: 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.

PubMed: 9761843
DOI: 10.1107/S090744499701216X

Experimental method

X-RAY DIFFRACTION (1.36 Å)