11ba

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:11ba.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:11ba.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_11ba| PDB=11ba | SCENE= }}
{{STRUCTURE_11ba| PDB=11ba | SCENE= }}
-
'''BINDING OF A SUBSTRATE ANALOGUE TO A DOMAIN SWAPPING PROTEIN IN THE COMPLEX OF BOVINE SEMINAL RIBONUCLEASE WITH URIDYLYL-2',5'-ADENOSINE'''
+
===BINDING OF A SUBSTRATE ANALOGUE TO A DOMAIN SWAPPING PROTEIN IN THE COMPLEX OF BOVINE SEMINAL RIBONUCLEASE WITH URIDYLYL-2',5'-ADENOSINE===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10082366}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10082366 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10082366}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Phosphoric diester]]
[[Category: Phosphoric diester]]
[[Category: Rna]]
[[Category: Rna]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:27:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:24:35 2008''

Revision as of 12:24, 30 June 2008

Image:11ba.png

Template:STRUCTURE 11ba

BINDING OF A SUBSTRATE ANALOGUE TO A DOMAIN SWAPPING PROTEIN IN THE COMPLEX OF BOVINE SEMINAL RIBONUCLEASE WITH URIDYLYL-2',5'-ADENOSINE

Template:ABSTRACT PUBMED 10082366

About this Structure

11BA is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

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., Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L, Protein Sci. 1998 Aug;7(8):1691-9. PMID:10082366

Page seeded by OCA on Mon Jun 30 15:24:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/11ba"
Personal tools