3DH5

Crystal structure of bovine pancreatic ribonuclease A (wild-type)

Summary for 3DH5

• Entry DOI: 10.2210/pdb3dh5/pdb
• Related: 3DH6 3DI7 3DI8 3DI9 3DIB 3DIC
• Descriptor: Ribonuclease pancreatic, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ribonuclease, rnase a, hydrolase, bovine pancreas, endonuclease, glycation, glycoprotein, nuclease, secreted
• Biological source: Bos taurus (bovine)
• Cellular location: Secreted: P61823
• Total number of polymer chains: 1
• Total formula weight: 13946.20

Authors

Kurpiewska, K.,Font, J.,Ribo, M.,Vilanova, M.,Lewinski, K. (deposition date: 2008-06-17, release date: 2008-07-15, Last modification date: 2024-11-20)

Primary citation

Kurpiewska, K.,Font, J.,Ribo, M.,Vilanova, M.,Lewinski, K.
X-ray crystallographic studies of RNase A variants engineered at the most destabilizing positions of the main hydrophobic core: further insight into protein stability
Proteins, 77:658-669, 2009

PubMed Abstract: To investigate the structural origin of decreased pressure and temperature stability, the crystal structure of bovine pancreatic ribonuclease A variants V47A, V54A, V57A, I81A, I106A, and V108A was solved at 1.4-2.0 A resolution and compared with the structure of wild-type protein. The introduced mutations had only minor influence on the global structure of ribonuclease A. The structural changes had individual character that depends on the localization of mutated residue, however, they seemed to expand from mutation site to the rest of the structure. Several different parameters have been evaluated to find correlation with decrease of free energy of unfolding DeltaDeltaG(T), and the most significant correlation was found for main cavity volume change. Analysis of the difference distance matrices revealed that the ribonuclease A molecule is organized into five relatively rigid subdomains with individual response to mutation. This behavior consistent with results of unfolding experiments is an intrinsic feature of ribonuclease A that might be surviving remnants of folding intermediates and reflects the dynamic nature of the molecule.

PubMed: 19544568
DOI: 10.1002/prot.22480

Experimental method

X-RAY DIFFRACTION (1.6 Å)