1rbs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rbs.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rbs.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rbs| PDB=1rbs | SCENE= }}
{{STRUCTURE_1rbs| PDB=1rbs | SCENE= }}
-
'''STRUCTURAL STUDY OF MUTANTS OF ESCHERICHIA COLI RIBONUCLEASE HI WITH ENHANCED THERMOSTABILITY'''
+
===STRUCTURAL STUDY OF MUTANTS OF ESCHERICHIA COLI RIBONUCLEASE HI WITH ENHANCED THERMOSTABILITY===
-
==Overview==
+
<!--
-
Systematic replacement of the amino acid residues in Escherichia coli ribonuclease HI with those in the thermophilic counterpart has revealed that two mutations, His62--&gt;Pro (H62P) and Lys95--&gt;Gly (K95G), increased the thermostability of the protein. These single-site mutant proteins, together with the mutant proteins His62--&gt;Ala (H62A), Lys95--&gt;Asn (K95N) and Lys95--&gt;Ala (K95A), were crystallized and their structures were determined at 1.8 A resolution. The crystal structures of these mutant proteins reveal that only the local structure around each mutation site is essential for the increase in thermostability. For each mutant protein, the stabilization mechanism is considered to be as follows: (i) H62P is stabilized because of a decrease in the entropy of the unfolded state, without a change in the native backbone structure; (ii) K95G is stabilized since the strain caused by the left-handed backbone structure in the typical 3:5 type loop is eliminated; and (iii) K95N is slightly stabilized by a hydrogen bond formed between the side-chain N delta-atom of the mutated aspargine residue and the main-chain carbonyl oxygen within the same residue.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8381958}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8381958 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8381958}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]
[[Category: Nakamura, H.]]
[[Category: Nakamura, H.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:18:41 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:37:09 2008''

Revision as of 10:37, 29 July 2008

Image:1rbs.png

Template:STRUCTURE 1rbs

STRUCTURAL STUDY OF MUTANTS OF ESCHERICHIA COLI RIBONUCLEASE HI WITH ENHANCED THERMOSTABILITY

Template:ABSTRACT PUBMED 8381958

About this Structure

1RBS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural study of mutants of Escherichia coli ribonuclease HI with enhanced thermostability., Ishikawa K, Kimura S, Kanaya S, Morikawa K, Nakamura H, Protein Eng. 1993 Jan;6(1):85-91. PMID:8381958

Page seeded by OCA on Tue Jul 29 13:37:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rbs"
Personal tools