Linked Life Data

11273698

Source:http://linkedlifedata.com/resource/pubmed/id/11273698

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-3-29
pubmed:databankReference
pubmed:abstractText
The type I dockerin domain is responsible for incorporating its associated glycosyl hydrolase into the bacterial cellulosome, a multienzyme cellulolytic complex, via its interaction with a receptor domain (cohesin domain) of the cellulosomal scaffolding subunit. The highly conserved dockerin domain is characterized by two Ca(2+)-binding sites with sequence similarity to the EF-hand motif. Here, we present the three-dimensional solution structure of the 69 residue dockerin domain of Clostridium thermocellum cellobiohydrolase CelS. Torsion angle dynamics calculations utilizing a total of 728 NOE-derived distance constraints and 79 torsion angle restraints yielded an ensemble of 20 structures with an average backbone r.m.s.d. for residues 5 to 29 and 32 to 66 of 0.54 A from the mean structure. The structure consists of two Ca(2+)-binding loop-helix motifs connected by a linker; the E helices entering each loop of the classical EF-hand motif are absent from the dockerin domain. Each dockerin Ca(2+)-binding subdomain is stabilized by a cluster of buried hydrophobic side-chains. Structural comparisons reveal that, in its non-complexed state, the dockerin fold displays a dramatic departure from that of Ca(2+)-bound EF-hand domains. A putative cohesin-binding surface, comprised of conserved hydrophobic and basic residues, is proposed, providing new insight into cellulosome assembly.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
307
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
745-53
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11273698-Amino Acid Sequence, pubmed-meshheading:11273698-Binding Sites, pubmed-meshheading:11273698-Calcium, pubmed-meshheading:11273698-Cell Cycle Proteins, pubmed-meshheading:11273698-Cellulase, pubmed-meshheading:11273698-Cellulose 1,4-beta-Cellobiosidase, pubmed-meshheading:11273698-Chromosomal Proteins, Non-Histone, pubmed-meshheading:11273698-Clostridium, pubmed-meshheading:11273698-EF Hand Motifs, pubmed-meshheading:11273698-Fungal Proteins, pubmed-meshheading:11273698-Models, Molecular, pubmed-meshheading:11273698-Molecular Sequence Data, pubmed-meshheading:11273698-Nuclear Magnetic Resonance, Biomolecular, pubmed-meshheading:11273698-Nuclear Proteins, pubmed-meshheading:11273698-Protein Binding, pubmed-meshheading:11273698-Protein Structure, Tertiary, pubmed-meshheading:11273698-Sequence Alignment
pubmed:year
2001
pubmed:articleTitle
Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.
pubmed:affiliation
Department of Chemical Engineering, University of Rochester, NY 14627-0166, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't