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.




1bsd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bsd.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1bsd.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bsd| PDB=1bsd | SCENE= }}
{{STRUCTURE_1bsd| PDB=1bsd | SCENE= }}
-
'''CRYSTAL STRUCTURAL ANALYSIS OF MUTATIONS IN THE HYDROPHOBIC CORES OF BARNASE'''
+
===CRYSTAL STRUCTURAL ANALYSIS OF MUTATIONS IN THE HYDROPHOBIC CORES OF BARNASE===
-
==Overview==
+
<!--
-
We have solved and analysed the crystal structures of five mutants in the hydrophobic core of barnase to investigate the structural basis for the contribution of hydrophobic residues and side-chain packing to the stability of globular proteins. In case ease, an amino acid side-chain has been replaced with one of smaller volume. The overall structures of four Ile--&gt;Val mutants (residues 51, 76, 88 and 96) and one Leu--&gt;Val mutant (residue 89) are all isomorphous with the wild-type structure. The magnitude and nature of structural shifts in the three hydrophobic core regions of barnase depend on the local environment of the substitution site, but have some features in common. (1) Side-chain atoms move to a greater extent than do main-chain atoms. (2) Repacking at the substitution site is achieved by either a rigid body shift of side-chain atoms (for Ile--&gt;Val76 and Ile--&gt;Val96 mutants), or by a combination of a side-chain shift and rotation (for Ile--&gt;Val51 and Ile--&gt;Val88 mutants). The mutated residue moves to the greatest extent, and generally in the direction of the created cavity (the largest atomic shift is 0.9 A, for Ile--&gt;Val51). The space left behind from such shifts is not seen to be filled by neighbouring side-chains. (3) Where a cavity remains after mutation, it does not contain any solvent molecules. (4) There is no correlation between the extent of structural movements and the atomic temperature factors of atoms that have moved. (5) Structural movements are not large enough to disrupt hydrogen bonding. Valine 88, in the Ile--&gt;Val88 mutant, is disordered and the electron density suggests several side-chain conformations. The reduction in the volumes of the cavities introduced upon mutation, due to collapse of the surrounding structure, ranges from 11% (Ile--&gt;Val96) to 90% (Ile--&gt;Val51).
+
The line below this paragraph, {{ABSTRACT_PUBMED_8254677}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8254677 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8254677}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Henrick, K.]]
[[Category: Henrick, K.]]
[[Category: Endonuclease]]
[[Category: Endonuclease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:53:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:38:56 2008''

Revision as of 16:38, 30 June 2008

Image:1bsd.png

Template:STRUCTURE 1bsd

CRYSTAL STRUCTURAL ANALYSIS OF MUTATIONS IN THE HYDROPHOBIC CORES OF BARNASE

Template:ABSTRACT PUBMED 8254677

About this Structure

1BSD is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

Crystal structural analysis of mutations in the hydrophobic cores of barnase., Buckle AM, Henrick K, Fersht AR, J Mol Biol. 1993 Dec 5;234(3):847-60. PMID:8254677

Page seeded by OCA on Mon Jun 30 19:38:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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