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9JWD

Crystal structure of RNAs A treated with sodium cyanide

Summary for 9JWD
Entry DOI10.2210/pdb9jwd/pdb
DescriptorRibonuclease pancreatic, CYANIDE ION, GLYCEROL, ... (6 entities in total)
Functional Keywordshydrolase
Biological sourceBos taurus (domestic cattle)
Total number of polymer chains1
Total formula weight14028.86
Authors
Ahmad, M.S.,Shah, N. (deposition date: 2024-10-10, release date: 2024-12-04)
Primary citationShah, N.,Akbar, Z.,Ahmad, M.S.
Cyanide mediated conformational changes resulted in the displacement of sulfate ion from the active site of bovine pancreatic ribonuclease A.
Biochem.Biophys.Res.Commun., 736:150868-150868, 2024
Cited by
PubMed Abstract: Ribonuclease A is a major hydrolyzing enzyme involved in the hydrolysis of RNA. The crystals of bovine pancreatic RNase A (bpRNase A) were grown at pH 5.5. The effect of sodium cyanide on bpRNase A was assessed by adding it directly to the crystal containing well. Treating the crystals of bpRNase A with sodium cyanide resulted in the displacement of the sulfate ion from the active site of bpRNase A, while the additional sulfate ion, bound to Ala-4, remained unaffected. The addition of sodium cyanide to bpRNase A crystals did not show change in the secondary structure elements of the enzyme. This study was conducted to check the effect of cyanide on bpRNase A crystals and to displace sulfate ion from its active site.
PubMed: 39490154
DOI: 10.1016/j.bbrc.2024.150868
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.22 Å)
Structure validation

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