Linked Life Data

9315852

Source:http://linkedlifedata.com/resource/pubmed/id/9315852

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
1997-10-23
pubmed:abstractText
A series of ATP analogs, in which moieties of various sizes have been added to the gamma-phosphorus of ATP, bind to the active site of myosin and to the actomyosin complex in myofibrils and in chemically skinned fibers. The affinity of the analogs for the active site shows only a slight dependence on the size of the added moiety. Addition of even our smallest group (CH3) reduced the binding affinity of ATPgamma-CH3 for S1 to 40 microM, a factor of 10(5) less than observed for ATP. Computer molecular docking of ATP-gammaCH3 into the myosin-ADP.BeF3 crystal structure of Dictyostelium discoideum indicates no steric interference to prevent binding. This suggests that the maintenance of charge at the gamma-phosphate is crucial for tight nucleotide binding. Addition of larger groups, (1) an EPR probe (ATP-gammaSL) or (2) ADP (i.e., P1, P5-diadenosine pentaphosphate, AP5A), reduced the affinity by only approximately a factor of 10 over that of ATP-gammaCH3. In the crystal structure of S1 complexed with nucleotides, the phosphates are buried within a protein structure called "the phosphate tube". Both the bulk of the modifying groups and the lack of dependence on the size of the group are incompatible with threading of the phosphates down the Pi-tube, showing that the tube must open. Similar domain movements have been found in other proteins including members of the G-protein superfamily, a family that has structural homologies to myosin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12155-66
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Opening of the myosin nucleotide triphosphate binding domain during the ATPase cycle.
pubmed:affiliation
Department of Pure and Applied Mathematics, Washington State University, Pullman 99164, USA. epate@wsu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.