Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
50
pubmed:dateCreated
2003-12-8
pubmed:abstractText
ClpX, a heat shock protein 100 chaperone, which acts as the regulatory subunit of the ATP-dependent ClpXP protease, is responsible for intracellular protein remodeling and degradation. To provide a structural basis for a better understanding of the function of the Clp ATPase family, the crystal structures of Helicobacter pylori ClpX, lacking an N-terminal Cys cluster region complexed with ADP, was determined. The overall structure of ClpX is similar to that of heat shock locus U (HslU), consisting of two subdomains, with ADP bound at the subdomain interface. The crystal structure of ClpX reveals that a conserved tripeptide (LGF) is located on the tip of ClpP binding loop extending from the N-terminal subdomain. A hexameric model of ClpX suggests that six tripeptides make hydrophobic contacts with the hydrophobic clefts of the ClpP heptmer asymmetrically. In addition, the nucleotide binding environment provides the structural explanation for the hexameric assembly and the modulation of ATPase activity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
50664-70
pubmed:dateRevised
2009-9-3
pubmed:meshHeading
pubmed-meshheading:14514695-Adenosine Diphosphate, pubmed-meshheading:14514695-Adenosine Triphosphatases, pubmed-meshheading:14514695-Amino Acid Sequence, pubmed-meshheading:14514695-Binding Sites, pubmed-meshheading:14514695-Crystallography, X-Ray, pubmed-meshheading:14514695-Endopeptidase Clp, pubmed-meshheading:14514695-Escherichia coli, pubmed-meshheading:14514695-Escherichia coli Proteins, pubmed-meshheading:14514695-Helicobacter pylori, pubmed-meshheading:14514695-Models, Molecular, pubmed-meshheading:14514695-Molecular Chaperones, pubmed-meshheading:14514695-Molecular Sequence Data, pubmed-meshheading:14514695-Nucleotides, pubmed-meshheading:14514695-Peptides, pubmed-meshheading:14514695-Protein Binding, pubmed-meshheading:14514695-Protein Conformation, pubmed-meshheading:14514695-Protein Structure, Tertiary
pubmed:year
2003
pubmed:articleTitle
Crystal structure of ClpX molecular chaperone from Helicobacter pylori.
pubmed:affiliation
Department of Molecular Cell Biology, Center for Molecular Medicine, SBRI, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't