Linked Life Data

8448199

Source:http://linkedlifedata.com/resource/pubmed/id/8448199

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1993-4-13
pubmed:abstractText
The 51-62 loop of T4 phage lysozyme was altered by site-directed mutagenesis to obtain maximal homology with the typical EF-hand motif. A Ca(2+)-binding site was designed and created by replacing both Gly-51 and Asn-53 with aspartic acid. The mutant T4 lysozyme (G51D/N53D) was expressed in Escherichia coli. The activity of the G51D/N53D-mutant was about 60% of that of the wild-type protein. This mutant can bind Ca2+ ions specifically, while the effective dissociation constant was essentially greater than that of the EF-hand proteins. Stability of the G51D/N53D-mutant apo-form to urea- or temperature-induced denaturation was the same as that of the wild-type protein. In the presence of Ca2+ ions in solution the stability of the mutant T4 phage lysozyme was less than that of the wild-type protein. It is suggested that the binding of Ca2+ by the mutant is accompanied by the considerable conformational changes in the 'corrected' loop, which can lead to the Ca(2+)-induced destabilization of the protein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
1162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
84-8
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Introduction of Ca(2+)-binding amino-acid sequence into the T4 lysozyme.
pubmed:affiliation
Institute of Protein Research, Academy of Sciences of Russia, Pushchino, Moscow Region.
pubmed:publicationType
Journal Article