Linked Life Data

11955057

Source:http://linkedlifedata.com/resource/pubmed/id/11955057

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2002-4-16
pubmed:abstractText
P22 tailspike is a homotrimeric, thermostable adhesin that recognizes the O-antigen lipopolysaccharide of Salmonella typhimurium. The 70 kDa subunits include long beta-helix domains. After residue 540, the polypeptide chains change their path and wrap around one another, with extensive interchain contacts. Formation of this interdigitated domain intimately couples the chain folding and assembly mechanisms. The earliest detectable trimeric intermediate in the tailspike folding and assembly pathway is the protrimer, suspected to be a precursor of the native trimer structure. We have directly analyzed the kinetics of in vitro protrimer formation and disappearance for wild type and mutant tailspike proteins. The results confirm that the protrimer intermediate is an on-pathway intermediate for tailspike folding. Protrimer was originally resolved during tailspike folding because its migration through nondenaturing polyacrylamide gels was significantly retarded with respect to the migration of the native tailspike trimer. By comparing protein mobility versus acrylamide concentration, we find that the retarded mobility of the protrimer is due exclusively to a larger overall size than the native trimer, rather than an altered net surface charge. Experiments with mutant tailspike proteins indicate that the conformation difference between protrimer and native tailspike trimer is localized toward the C-termini of the tailspike polypeptide chains. These results suggest that the transformation of the protrimer to the native tailspike trimer represents the C-terminal interdigitation of the three polypeptide chains. This late step may confer the detergent-resistance, protease-resistance, and thermostability of the native trimer.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5093-103
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:11955057-Amino Acid Substitution, pubmed-meshheading:11955057-Arginine, pubmed-meshheading:11955057-Bacteriophage P22, pubmed-meshheading:11955057-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:11955057-Evolution, Molecular, pubmed-meshheading:11955057-Glutathione, pubmed-meshheading:11955057-Glycine, pubmed-meshheading:11955057-Glycoside Hydrolases, pubmed-meshheading:11955057-Kinetics, pubmed-meshheading:11955057-Oxidation-Reduction, pubmed-meshheading:11955057-Point Mutation, pubmed-meshheading:11955057-Protein Conformation, pubmed-meshheading:11955057-Protein Folding, pubmed-meshheading:11955057-Protein Structure, Secondary, pubmed-meshheading:11955057-Salmonella typhimurium, pubmed-meshheading:11955057-Surface Properties, pubmed-meshheading:11955057-Temperature, pubmed-meshheading:11955057-Viral Tail Proteins
pubmed:year
2002
pubmed:articleTitle
Characterization of the protrimer intermediate in the folding pathway of the interdigitated beta-helix tailspike protein.
pubmed:affiliation
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't