254l: Difference between revisions

Revision as of 06:28, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:254l.png

Template:STRUCTURE 254l

LYSOZYMELYSOZYME

Template:ABSTRACT PUBMED 7831309

About this StructureAbout this Structure

254L is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

ReferenceReference

A relationship between protein stability and protein function., Shoichet BK, Baase WA, Kuroki R, Matthews BW, Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):452-6. PMID:7831309

Page seeded by OCA on Tue Jul 29 06:28:19 2008

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OCA

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-==Overview==
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-Enzymes are thought to use their ordered structures to facilitate catalysis. A corollary of this theory suggests that enzyme residues involved in function are not optimized for stability. We tested this hypothesis by mutating functionally important residues in the active site of T4 lysozyme. Six mutations at two catalytic residues, Glu-11 and Asp-20, abolished or reduced enzymatic activity but increased thermal stability by 0.7-1.7 kcal.mol-1. Nine mutations at two substrate-binding residues, Ser-117 and Asn-132, increased stability by 1.2-2.0 kcal.mol-1, again at the cost of reduced activity. X-ray crystal structures show that the substituted residues complement regions of the protein surface that are used for substrate recognition in the native enzyme. In two of these structures the enzyme undergoes a general conformational change, similar to that seen in an enzyme-product complex. These results support a relationship between stability and function for T4 lysozyme. Other evidence suggests that the relationship is general.
+The line below this paragraph, {{ABSTRACT_PUBMED_7831309}}, adds the Publication Abstract to the page
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 [[Category: Glycosidase]]
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