From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1rcn.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rcn.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1rcn| PDB=1rcn | SCENE= }} | | {{STRUCTURE_1rcn| PDB=1rcn | SCENE= }} |
| | | | |
| - | '''CRYSTAL STRUCTURE OF THE RIBONUCLEASE A D(APTPAPAPG) COMPLEX : DIRECT EVIDENCE FOR EXTENDED SUBSTRATE RECOGNITION'''
| + | ===CRYSTAL STRUCTURE OF THE RIBONUCLEASE A D(APTPAPAPG) COMPLEX : DIRECT EVIDENCE FOR EXTENDED SUBSTRATE RECOGNITION=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The crystal structure of the complex between ribonuclease A and d(ApTpApApG) has been solved by x-ray crystallography using the molecular replacement method. The model includes, besides the enzyme, the d(ApTpApA) 5'-segment (A1T2A3A4) and 68 solvent molecules. The R-factor for the strongest 87% of the measured data that partially extends to 2.3-A resolution is 0.207. The A1 position is well defined; the 5'-O of the deoxyribose establishes a hydrogen bond with a solvent molecule that is, in turn, bonded to the epsilon-amino group of Lys66. The base (B0 site) is well ordered; it interacts with a symmetry-related enzyme molecule. In the crystal, the phosphate group at the p0 site has no direct charge compensation. However, Lys66 is not too far, and, in solution, it could bind to it. The T2 (R1B1p1) site is occupied as in other complex structures, and it is defined by very good electron density. The A3 site shows that the adenine moiety interacts with Asn71 and Gln69 and that the phosphate at p2 forms a salt bridge with Lys7. The most consistent model for the base of A4 (B3), both in terms of electron density and stereochemistry, shows that it forms a hydrogen bond with Gln69 and a g-g- array with the base at B2. The stacking of B2 and B3 may be a general feature of the binding of polyribonucleotides to ribonuclease A. The side chains of Gln69, Asn71, and Glu111 may thus constitute a malleable binding site capable of establishing various hydrogen bonds depending on the nature of the stacked bases. There is no evidence for the 3' G5 site in the electron density map. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8063789}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8063789 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_8063789}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 28: |
Line 32: |
| | [[Category: Llorens, R De.]] | | [[Category: Llorens, R De.]] |
| | [[Category: Protein-dna complex]] | | [[Category: Protein-dna complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:20:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:33:10 2008'' |
Revision as of 04:33, 28 July 2008
Template:STRUCTURE 1rcn
CRYSTAL STRUCTURE OF THE RIBONUCLEASE A D(APTPAPAPG) COMPLEX : DIRECT EVIDENCE FOR EXTENDED SUBSTRATE RECOGNITION
Template:ABSTRACT PUBMED 8063789
About this Structure
1RCN is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Crystal structure of ribonuclease A.d(ApTpApApG) complex. Direct evidence for extended substrate recognition., Fontecilla-Camps JC, de Llorens R, le Du MH, Cuchillo CM, J Biol Chem. 1994 Aug 26;269(34):21526-31. PMID:8063789
Page seeded by OCA on Mon Jul 28 07:33:10 2008
