Linked Life Data

15328341

Source:http://linkedlifedata.com/resource/pubmed/id/15328341

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
2004-11-1
pubmed:databankReference
pubmed:abstractText
E2 conjugating enzymes form a thiol ester intermediate with ubiquitin, which is subsequently transferred to a substrate protein targeted for degradation. While all E2 proteins comprise a catalytic domain where the thiol ester is formed, several E2s (class II) have C-terminal extensions proposed to control substrate recognition, dimerization, or polyubiquitin chain formation. Here we present the novel solution structure of the class II E2 conjugating enzyme Ubc1 from Saccharomyces cerevisiae. The structure shows the N-terminal catalytic domain adopts an alpha/beta fold typical of other E2 proteins. This domain is physically separated from its C-terminal domain by a 22-residue flexible tether. The C-terminal domain adopts a three-helix bundle that we have identified as an ubiquitin-associated domain (UBA). NMR chemical shift perturbation experiments show this UBA domain interacts in a regioselective manner with ubiquitin. This two-domain structure of Ubc1 was used to identify other UBA-containing class II E2 proteins, including human E2-25K, that likely have a similar architecture and to determine the role of the UBA domain in facilitating polyubiquitin chain formation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47139-47
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15328341-Amino Acid Sequence, pubmed-meshheading:15328341-Binding Sites, pubmed-meshheading:15328341-Catalytic Domain, pubmed-meshheading:15328341-Dimerization, pubmed-meshheading:15328341-Dose-Response Relationship, Drug, pubmed-meshheading:15328341-Humans, pubmed-meshheading:15328341-Lysine, pubmed-meshheading:15328341-Magnetic Resonance Spectroscopy, pubmed-meshheading:15328341-Models, Molecular, pubmed-meshheading:15328341-Molecular Sequence Data, pubmed-meshheading:15328341-Protein Conformation, pubmed-meshheading:15328341-Protein Structure, Tertiary, pubmed-meshheading:15328341-Saccharomyces cerevisiae, pubmed-meshheading:15328341-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15328341-Sequence Homology, Amino Acid, pubmed-meshheading:15328341-Ubiquitin, pubmed-meshheading:15328341-Ubiquitin-Conjugating Enzymes
pubmed:year
2004
pubmed:articleTitle
Solution structure of the flexible class II ubiquitin-conjugating enzyme Ubc1 provides insights for polyubiquitin chain assembly.
pubmed:affiliation
Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't