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.


1lli

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lli.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lli.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lli| PDB=1lli | SCENE= }}
{{STRUCTURE_1lli| PDB=1lli | SCENE= }}
-
'''THE CRYSTAL STRUCTURE OF A MUTANT PROTEIN WITH ALTERED BUT IMPROVED HYDROPHOBIC CORE PACKING'''
+
===THE CRYSTAL STRUCTURE OF A MUTANT PROTEIN WITH ALTERED BUT IMPROVED HYDROPHOBIC CORE PACKING===
-
==Overview==
+
<!--
-
The dense packing observed in protein interiors appears to be crucial for stabilizing the native structure--even subtle internal substitutions are usually destabilizing. Thus, steric complementarity of core residues is thought to be an important criterion for "inverse folding" predictive methods, which judge whether a newly determined sequence is consistent with any known folds. A major problem in the development of useful core packing evaluation algorithms, however, is that there are occasional mutations that are predicted to disrupt native packing but that yield an equally or more stable protein. We have solved the crystal structure of such a variant of lambda repressor, which, despite having three larger core substitutions, is more stable than the wild type. The structure reveals that the protein accommodates the potentially disruptive residues with shifts in its alpha-helical arrangement. The variant is apparently more stable because its packing is improved--the core has a higher packing density and little geometric strain. These rearrangements, however, cause repositioning of functional residues, which result in reduced DNA binding activity. By comparing these results with the predictions of two core packing algorithms, it is clear that the protein possesses a relatively high degree of main-chain flexibility that must be accounted for in order to predict the full spectrum of compatible core sequences. This study also shows how, in protein evolution, a particular set of core residue identities might be selected not because they provide optimal stability but because they provide sufficient stability in addition to the precise structure required for optimal activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8278404}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8278404 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8278404}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Double helix]]
[[Category: Double helix]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:02:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:22:47 2008''

Revision as of 18:22, 2 July 2008

Image:1lli.png

Template:STRUCTURE 1lli

THE CRYSTAL STRUCTURE OF A MUTANT PROTEIN WITH ALTERED BUT IMPROVED HYDROPHOBIC CORE PACKING

Template:ABSTRACT PUBMED 8278404

About this Structure

1LLI is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.

Reference

The crystal structure of a mutant protein with altered but improved hydrophobic core packing., Lim WA, Hodel A, Sauer RT, Richards FM, Proc Natl Acad Sci U S A. 1994 Jan 4;91(1):423-7. PMID:8278404

Page seeded by OCA on Wed Jul 2 21:22:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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