11BA
BINDING OF A SUBSTRATE ANALOGUE TO A DOMAIN SWAPPING PROTEIN IN THE COMPLEX OF BOVINE SEMINAL RIBONUCLEASE WITH URIDYLYL-2',5'-ADENOSINE
Summary for 11BA
| Entry DOI | 10.2210/pdb11ba/pdb |
| Descriptor | PROTEIN (RIBONUCLEASE, SEMINAL), SULFATE ION, URIDYLYL-2'-5'-PHOSPHO-ADENOSINE, ... (4 entities in total) |
| Functional Keywords | hydrolase, phosphoric diester, rna, 2'-5'-dinucleotide |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 2 |
| Total formula weight | 28700.28 |
| Authors | Vitagliano, L.,Adinolfi, S.,Riccio, A.,Sica, F.,Zagari, A.,Mazzarella, L. (deposition date: 1999-03-17, release date: 1999-03-26, Last modification date: 2024-11-20) |
| Primary citation | Vitagliano, L.,Adinolfi, S.,Riccio, A.,Sica, F.,Zagari, A.,Mazzarella, L. Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2',5')adenosine. Protein Sci., 7:1691-1699, 1998 Cited by PubMed Abstract: Bovine seminal ribonuclease (BS-RNase) is a unique member of the pancreatic-like ribonuclease superfamily. The native enzyme is a mixture of two dimeric forms with distinct structural features. The most abundant form is characterized by the swapping of N-terminal fragments. In this paper, the crystal structure of the complex between the swapping dimer and uridylyl(2',5')adenosine is reported at 2.06 A resolution. The refined model has a crystallographic R-factor of 0.184 and good stereochemistry. The quality of the electron density maps enables the structure of both the inhibitor and active site residues to be unambiguously determined. The overall architecture of the active site is similar to that of RNase A. The dinucleotide adopts an extended conformation with the pyrimidine and purine base interacting with Thr45 and Asn71, respectively. Several residues (Gln11, His12, Lys41, His119, and Phe120) bind the oxygens of the phosphate group. The structural similarity of the active sites of BS-RNase and RNase A includes some specific water molecules believed to be relevant to catalytic activity. Upon binding of the dinucleotide, small but significant modifications of the tertiary and quaternary structure of the protein are observed. The ensuing correlation of these modifications with the catalytic activity of the enzyme is discussed. PubMed: 10082366DOI: 10.1002/pro.5560070804 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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