Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2008-6-9
pubmed:databankReference
pubmed:abstractText
The Mini-Chromosome Maintenance (MCM) proteins are candidates of replicative DNA helicase in eukarya and archaea. Here we report a 2.8 A crystal structure of the N-terminal domain (residues 1-268) of the Sulfolobus solfataricus MCM (Sso MCM) protein. The structure reveals single-hexameric ring-like architecture, at variance from the protein of Methanothermobacter thermoautotrophicus (Mth). Moreover, the central channel in Sso MCM seems significantly narrower than the Mth counterpart, which appears to more favorably accommodate single-stranded DNA than double-stranded DNA, as supported by DNA-binding assays. Structural analysis also highlights the essential role played by the zinc-binding domain in the interaction with nucleic acids and allows us to speculate that the Sso MCM N-ter domain may function as a molecular clamp to grasp the single-stranded DNA passing through the central channel. On this basis possible DNA unwinding mechanisms are discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-10611290, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-10677495, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-10872463, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-11606589, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-11821426, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-12151340, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-12524516, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-12527760, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-12548282, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-12774115, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-12907732, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-14527289, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-14566326, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15007098, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15024075, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15100218, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15140883, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15299926, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15304224, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15342486, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15371413, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15608193, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15670590, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15805601, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-15917436, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16002295, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16116441, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16218703, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16221679, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16221680, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16284270, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16679413, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16689629, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-16855583, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-17062628, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-17259218, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-17337732, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-17506634, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-17884823, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-17895243, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-17964268, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-7731998, http://linkedlifedata.com/resource/pubmed/commentcorrection/18417534-9305914
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1362-4962
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3235-43
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:18417534-Amino Acid Sequence, pubmed-meshheading:18417534-Archaeal Proteins, pubmed-meshheading:18417534-Bacterial Proteins, pubmed-meshheading:18417534-Binding Sites, pubmed-meshheading:18417534-Crystallography, X-Ray, pubmed-meshheading:18417534-DNA Helicases, pubmed-meshheading:18417534-DNA-Binding Proteins, pubmed-meshheading:18417534-Methanobacteriaceae, pubmed-meshheading:18417534-Models, Molecular, pubmed-meshheading:18417534-Molecular Sequence Data, pubmed-meshheading:18417534-Protein Structure, Secondary, pubmed-meshheading:18417534-Protein Structure, Tertiary, pubmed-meshheading:18417534-Protein Subunits, pubmed-meshheading:18417534-Sequence Deletion, pubmed-meshheading:18417534-Structural Homology, Protein, pubmed-meshheading:18417534-Sulfolobus solfataricus, pubmed-meshheading:18417534-Zinc
pubmed:year
2008
pubmed:articleTitle
Structural analysis of the Sulfolobus solfataricus MCM protein N-terminal domain.
pubmed:affiliation
Center of Structural Biochemistry, Karolinska Institutet NOVUM, 141 57 Huddinge, Sweden. wei.liu@ki.se
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't