This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5rnt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:5rnt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:5rnt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_5rnt| PDB=5rnt | SCENE= }}
{{STRUCTURE_5rnt| PDB=5rnt | SCENE= }}
-
'''X-RAY ANALYSIS OF CUBIC CRYSTALS OF THE COMPLEX FORMED BETWEEN RIBONUCLEASE T1 AND GUANOSINE-3',5'-BISPHOSPHATE'''
+
===X-RAY ANALYSIS OF CUBIC CRYSTALS OF THE COMPLEX FORMED BETWEEN RIBONUCLEASE T1 AND GUANOSINE-3',5'-BISPHOSPHATE===
-
==Overview==
+
<!--
-
The complex formed between ribonuclease T1 (RNase T1) and guanosine-3',5'-bisphosphate (3',5'-pGp) crystallizes in the cubic space group I23 with alpha = 86.47 (4) A. X-ray data were collected on a four-circle diffractometer to 3.2 A resolution and the structure was determined by molecular-replacement methods [ULTIMA; Rabinovich &amp; Shakked (1984). Acta Cryst. A40, 195-200] based on the RNase T1 coordinates taken from the complex with guanosine-2'-phosphate. Refinement converged at 16.6% for 1540 data with Fo greater than 1 sigma (Fo) with acceptable stereochemistry. The RNase T1 conformation is comparable to that in other complexes which crystallize preferentially in space group P2(1)2(1)2(1) except for side chains that interact intermolecularly. The guanine of 3',5'-pGp is bound to the recognition site in the same way as in other guanine-containing complexes except for its interaction with Glu46. The side-chain carboxylate of this amino acid does not form hydrogen bonds to N1H and N2H of guanine but is rotated so as to permit insertion of two water molecules which replace its acceptor functions. In contrast to other guanosine derivatives which are bound to RNase T1 in the syn form, 3',5'-pGp is anti. This conformation positions the two phosphate groups 'outside' the protein, with hydrogen-bonding contacts only to water molecules; the active site is filled by water. The RNase T1-3',5'-pGp complex probably has biological significance as it may represent the enzyme-product complex before dissociation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1930833}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1930833 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1930833}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Lenz, A.]]
[[Category: Lenz, A.]]
[[Category: Saenger, W.]]
[[Category: Saenger, W.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:37:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:10:38 2008''

Revision as of 11:10, 3 July 2008

Image:5rnt.png

Template:STRUCTURE 5rnt

X-RAY ANALYSIS OF CUBIC CRYSTALS OF THE COMPLEX FORMED BETWEEN RIBONUCLEASE T1 AND GUANOSINE-3',5'-BISPHOSPHATE

Template:ABSTRACT PUBMED 1930833

About this Structure

5RNT is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.

Reference

X-ray analysis of cubic crystals of the complex formed between ribonuclease T1 and guanosine-3',5'-bisphosphate., Lenz A, Heinemann U, Maslowska M, Saenger W, Acta Crystallogr B. 1991 Aug 1;47 ( Pt 4):521-7. PMID:1930833

Page seeded by OCA on Thu Jul 3 14:10:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5rnt"
Personal tools