2op2

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Crystal structure of RNase double-mutant V43C R85C with extra disulphide bond

Structural highlights

2op2 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 1.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1]

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

A previously introduced kinetic-rate constant (k/k(0)) method, where k and k(0) are the folding (unfolding) rate constants in the mutant and the wild-type forms, respectively, of a protein, has been applied to obtain qualitative information about structure in the transition state ensemble (TSE) of bovine pancreatic ribonuclease A (RNase A), which contains four native disulfide bonds. The method compares the folding (unfolding) kinetics of RNase A, with and without a covalent crosslink and tests whether the crosslinked residues are associated in the folding (unfolding) transition state (TS) of the noncrosslinked version. To confirm that the fifth disulfide bond has not introduced a significant structural perturbation, we solved the crystal structure of the V43C-R85C mutant to 1.6 A resolution. Our findings suggest that residues Val43 and Arg85 are not associated, and that residues Ala4 and Val118 may form nonnative contacts, in the folding (unfolding) TSE of RNase A.

Implementation of a k/k(0) method to identify long-range structure in transition states during conformational folding/unfolding of proteins.,Pradeep L, Kurinov I, Ealick SE, Scheraga HA Structure. 2007 Oct;15(10):1178-89. PMID:17937908[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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The effect of additional disulfide bonds on the stability and folding of ribonuclease A.
Pecher et al. (2009)
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1 other articles
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See Also

References

  1. ↑ delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
  2. ↑ Pradeep L, Kurinov I, Ealick SE, Scheraga HA. Implementation of a k/k(0) method to identify long-range structure in transition states during conformational folding/unfolding of proteins. Structure. 2007 Oct;15(10):1178-89. PMID:17937908 doi:10.1016/j.str.2007.08.003

Contents


PDB ID 2op2

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OCA

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