1l16: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1l16.jpg|left|200px]]
{{Seed}}
[[Image:1l16.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1l16|  PDB=1l16  |  SCENE=  }}  
{{STRUCTURE_1l16|  PDB=1l16  |  SCENE=  }}  


'''STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTERIOPHAGE T4 LYSOZYME, GLYCINE 156 (RIGHT ARROW) ASPARTIC ACID'''
===STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTERIOPHAGE T4 LYSOZYME, GLYCINE 156 (RIGHT ARROW) ASPARTIC ACID===




==Overview==
<!--  
The structure of the mutant of bacteriophage T4 lysozyme in which Gly-156 is replaced by aspartic acid is described. The lysozyme was isolated by screening for temperature-sensitive mutants and has a melting temperature at pH 6.5 that is 6.1 degrees C lower than wild type. The mutant structure is destabilized, in part, because Gly-156 has conformational angles (phi, psi) that are not optimal for a residue with a beta-carbon. High resolution crystallographic refinement of the mutant structure (R = 17.7% at 1.7 A resolution) shows that the Gly----Asp substitution does not significantly alter the configurational angles (phi, psi) but forces the backbone to move, as a whole, approximately 0.6 A away from its position in wild-type lysozyme. This induced strain weakens a hydrogen bond network that exists in the wild-type structure and also contributes to the reduced stability of the mutant lysozyme. The introduction of an acidic side chain reduces the overall charge on the molecule and thereby tends to increase the stability of the mutant structure relative to wild type. However, at neutral pH this generalized electrostatic stabilization is offset by specific electrostatic repulsion between Asp-156 and Asp-92. The activity of the mutant lysozyme is approximately 50% that of wild-type lysozyme. This reduction in activity might be due to introduction of a negative charge and/or perturbation of the surface of the molecule in the region that is assumed to interact with peptidoglycan substrates.
The line below this paragraph, {{ABSTRACT_PUBMED_3680274}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 3680274 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_3680274}}


==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Gray, T M.]]
[[Category: Gray, T M.]]
[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:25:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:28:19 2008''

Revision as of 08:28, 2 July 2008

File:1l16.png

Template:STRUCTURE 1l16

STRUCTURAL ANALYSIS OF THE TEMPERATURE-SENSITIVE MUTANT OF BACTERIOPHAGE T4 LYSOZYME, GLYCINE 156 (RIGHT ARROW) ASPARTIC ACID

Template:ABSTRACT PUBMED 3680274

About this Structure

1L16 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

Structural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid., Gray TM, Matthews BW, J Biol Chem. 1987 Dec 15;262(35):16858-64. PMID:3680274

Page seeded by OCA on Wed Jul 2 11:28:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1l16&oldid=623434"