Linked Life Data

18796009

Source:http://linkedlifedata.com/resource/pubmed/id/18796009

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2009-3-13
pubmed:abstractText
SKD1/VPS4B belongs to the adenosine triphosphatases associated with diverse cellular activities (AAA) family and regulates multivesicular body (MVB) biogenesis. SKD1 changes its oligomeric state during the ATPase cycle and subsequently releases endosomal sorting complex required for transport (ESCRT) complexes from endosomes during the formation of MVBs. In this study, we describe domain motions in monomeric SKD1 on ATP and ADP binding. Nucleotides bind between the alpha/beta and the alpha-helical domains of SKD1, inducing a approximately 20 degrees domain rotation and closure of the binding site, which are similar to the changes observed in the AAA+ ATPase, HslU. Gel filtration and small-angle X-ray scattering experiments showed that the ATP-bound form of SKD1 oligomerizes in solution, whereas ADP-bound and apo forms of SKD1 exist as monomers, even though the conformations of the ADP- and ATP-bound forms are nearly identical. Nucleotide-bound SKD1 structures are compatible with a hexameric ring arrangement reminiscent of the AAA ATPase p97 D1 ring. In the hexameric ring model of SKD1, Arg290 from a neighboring molecule binds to the gamma-phosphate of ATP, which promotes oligomerization of the ATP-bound form. ATP hydrolysis would eliminate this interaction and subsequent nucleotide release causes the domains to rotate, which together lead to the disassembly of the SKD1 oligomer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1600-0854
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2180-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18796009-Adenosine Triphosphatases, pubmed-meshheading:18796009-Animals, pubmed-meshheading:18796009-Arginine, pubmed-meshheading:18796009-Binding Sites, pubmed-meshheading:18796009-Chromatography, Gel, pubmed-meshheading:18796009-Crystallography, X-Ray, pubmed-meshheading:18796009-Endosomal Sorting Complexes Required for Transport, pubmed-meshheading:18796009-Humans, pubmed-meshheading:18796009-Hydrolysis, pubmed-meshheading:18796009-Mice, pubmed-meshheading:18796009-Models, Molecular, pubmed-meshheading:18796009-Molecular Weight, pubmed-meshheading:18796009-Nucleotides, pubmed-meshheading:18796009-Protein Binding, pubmed-meshheading:18796009-Protein Multimerization, pubmed-meshheading:18796009-Protein Structure, Quaternary, pubmed-meshheading:18796009-Protein Structure, Tertiary, pubmed-meshheading:18796009-Repressor Proteins, pubmed-meshheading:18796009-Saccharomyces cerevisiae, pubmed-meshheading:18796009-Saccharomyces cerevisiae Proteins, pubmed-meshheading:18796009-Vesicular Transport Proteins
pubmed:year
2008
pubmed:articleTitle
Nucleotide-dependent conformational changes and assembly of the AAA ATPase SKD1/VPS4B.
pubmed:affiliation
Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-0801, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't