We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

5bir

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:5bir.gif|left|200px]]
+
{{Seed}}
 +
[[Image:5bir.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_5bir| PDB=5bir | SCENE= }}
{{STRUCTURE_5bir| PDB=5bir | SCENE= }}
-
'''DISECTING HISTIDINE INTERACTIONS IN RIBONUCLEASE T1 USING ASN AND GLN MUTATIONS'''
+
===DISECTING HISTIDINE INTERACTIONS IN RIBONUCLEASE T1 USING ASN AND GLN MUTATIONS===
-
==Overview==
+
<!--
-
His92 of Ribonuclease T1 combines functional and structural features involving both imidazole nitrogens. To evaluate the use of Asn and Gln substitutions in dissecting the properties of histidines, we analysed the consequences of the His92Gln and His92Asn substitutions on the enzyme's structure, function, and conformational stability by protein engineering and X-ray crystallographic methods. In the X-ray structures of wild-type and His92Gln RNase T1 in complex with 2'-GMP the His92-N epsilon 2 and Gln92-N epsilon 2 atoms are isosterically equivalent. Similarly, the His92N delta 1H...OAsn99 hydrogen bond observed in wild-type is replaced by an equivalent Asn92N delta 2H...OAsn99 in the His92Asn mutant structure. Double mutant cycles at a single position were used to analyse the intermolecular and intramolecular interactions of the exchangeable proton and the individual histidine nitrogens. Urea denaturation measurements as a function of pH revealed that the exchangeable proton of His92, rather than its imidazole ring is contributing about 1 kcal/mol to the conformational stability of RNase T1. The stabilizing and the destabilizing effects of the (His--&gt;Gln) and the (His--&gt;Asn) mutations on urea denaturation of RNase T1 at pH 9.0 suggest that the unprotonated N delta 1 and N epsilon 2 atoms contribute in a compensating way to the conformational stability of RNase T1. A comparative study of the kinetics of all mutants suggests that the protonated His92 imidazole is a strictly co-operative catalytic device.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9466938}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9466938 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9466938}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Mutation]]
[[Category: Mutation]]
[[Category: Ribonuclease t1]]
[[Category: Ribonuclease t1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:32:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:56:53 2008''

Revision as of 10:56, 3 July 2008

Image:5bir.png

Template:STRUCTURE 5bir

DISECTING HISTIDINE INTERACTIONS IN RIBONUCLEASE T1 USING ASN AND GLN MUTATIONS

Template:ABSTRACT PUBMED 9466938

About this Structure

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

Reference

Dissecting histidine interactions of ribonuclease T1 with asparagine and glutamine replacements: analysis of double mutant cycles at one position., De Vos S, Doumen J, Langhorst U, Steyaert J, J Mol Biol. 1998 Jan 30;275(4):651-61. PMID:9466938

Page seeded by OCA on Thu Jul 3 13:56:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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