Linked Life Data

7031058

Source:http://linkedlifedata.com/resource/pubmed/id/7031058

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1982-2-22
pubmed:abstractText
The technique of small angle x-ray scattering has been employed to study the effect of sugars on the radius of gyration of the L-arabinose-binding protein, a component of the high affinity L-arabinose transport system in Escherichia coli. We find that the binding of L-arabinose to the "sugar-free" protein in solution causes a 0.94 +/- 0.33 A decrease in the radius of gyration while D-glucose, a nonbinder, produces no such effect. The radius of gyration calculated from the complete atomic co-ordinates of the crystal structure of L-arabinose-binding protein (solved with bound L-arabinose) corresponds to the experimentally determined value for the radius of gyration in the presence of L-arabinose. This reduction in radius of gyration can be best accounted for in terms of a substrate-induced cleft closure in which one lobe rotates relative to the other lobe. A compute modeling study indicates that a rotation of 18 degrees about a hinge deep in the base of the sugar-binding cleft between the two domains would produce the observed decrease in the radius of gyration. The findings (Newcomer, M. E., Gilliland, G. L., and Quiocho, F. A. (1981) J. Biol. Chem. 256, 13213-13222) that the L-arabinose molecule embedded in the cleft between two domains is completely inaccessible to the solvent is consistent with a closing of the cleft between the two lobes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13218-22
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
The radius of gyration of L-arabinose-binding protein decreases upon binding of ligand.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't