Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-1-14
pubmed:databankReference
pubmed:abstractText
The ROP2 protein and its paralogs are important virulence factors secreted into the host cell by the parasite Toxoplasma gondii. Here we describe the crystal structure of a large and soluble domain of mature ROP2, representative of the ROP2-like protein family. This is a structure of a protein-kinase fold that is devoid of catalytic residues and does not bind ATP. Various structural extensions constitute a signature of this protein family and act to maintain the protein kinase in an open conformation. Our ROP2 structure rules out a previous structural model of attachment of ROP2-like proteins to the parasitophorous vacuole membrane. We propose an alternative mode of membrane attachment implicating basic and amphiphatic helices present in the flexible N terminus of ROP2.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-46
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:19141290-Amino Acid Sequence, pubmed-meshheading:19141290-Animals, pubmed-meshheading:19141290-Base Sequence, pubmed-meshheading:19141290-Binding Sites, pubmed-meshheading:19141290-Cell Line, pubmed-meshheading:19141290-Circular Dichroism, pubmed-meshheading:19141290-Cricetinae, pubmed-meshheading:19141290-DNA Primers, pubmed-meshheading:19141290-Membrane Proteins, pubmed-meshheading:19141290-Models, Molecular, pubmed-meshheading:19141290-Molecular Sequence Data, pubmed-meshheading:19141290-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:19141290-Peptides, pubmed-meshheading:19141290-Protein Folding, pubmed-meshheading:19141290-Protein Kinases, pubmed-meshheading:19141290-Protozoan Proteins, pubmed-meshheading:19141290-Sequence Homology, Amino Acid, pubmed-meshheading:19141290-Toxoplasma, pubmed-meshheading:19141290-Virulence
pubmed:year
2009
pubmed:articleTitle
ROP2 from Toxoplasma gondii: a virulence factor with a protein-kinase fold and no enzymatic activity.
pubmed:affiliation
Atelier de Bio- et Chimie Informatique Structurale, Centre de Biochimie Structurale, CNRS, UMR5048, Universités Montpellier 1 et 2, F34090 Montpellier, France. labesse@cbs.cnrs.fr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't