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.

1ob0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ob0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ob0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ob0| PDB=1ob0 | SCENE= }}
{{STRUCTURE_1ob0| PDB=1ob0 | SCENE= }}
-
'''KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE'''
+
===KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE===
-
==Overview==
+
<!--
-
It is generally assumed that in proteins hydrophobic residues are not favorable at solvent-exposed sites, and that amino acid substitutions on the surface have little effect on protein thermostability. Contrary to these assumptions, we have identified hyperthermostable variants of Bacillus licheniformis alpha-amylase (BLA) that result from the incorporation of hydrophobic residues at the surface. Under highly destabilizing conditions, a variant combining five stabilizing mutations unfolds 32 times more slowly and at a temperature 13 degrees C higher than the wild-type. Crystal structure analysis at 1.7 A resolution suggests that stabilization is achieved through (a) extension of the concept of increased hydrophobic packing, usually applied to cavities, to surface indentations, (b) introduction of favorable aromatic-aromatic interactions on the surface, (c) specific stabilization of intrinsic metal binding sites, and (d) stabilization of a beta-sheet by introducing a residue with high beta-sheet forming propensity. All mutated residues are involved in forming complex, cooperative interaction networks that extend from the interior of the protein to its surface and which may therefore constitute "weak points" where BLA unfolding is initiated. This might explain the unexpectedly large effect induced by some of the substitutions on the kinetic stability of BLA. Our study shows that substantial protein stabilization can be achieved by stabilizing surface positions that participate in underlying cooperatively formed substructures. At such positions, even the apparently thermodynamically unfavorable introduction of hydrophobic residues should be explored.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12540849}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12540849 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12540849}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Starch degradation]]
[[Category: Starch degradation]]
[[Category: Thermostability]]
[[Category: Thermostability]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:36:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:47:23 2008''

Revision as of 04:47, 29 July 2008

Image:1ob0.png

Template:STRUCTURE 1ob0

KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE

Template:ABSTRACT PUBMED 12540849

About this Structure

1OB0 is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.

Reference

Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface., Machius M, Declerck N, Huber R, Wiegand G, J Biol Chem. 2003 Mar 28;278(13):11546-53. Epub 2003 Jan 21. PMID:12540849

Page seeded by OCA on Tue Jul 29 07:47:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ob0"
Personal tools