Linked Life Data

8310056

Source:http://linkedlifedata.com/resource/pubmed/id/8310056

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1994-3-11
pubmed:abstractText
The three-dimensional structure of the vicilin storage protein canavalin, from Canavalia ensiformis, has been determined in a hexagonal crystal by x-ray diffraction methods. The model has been refined at 2.6 A resolution to an R factor of 0.197 with acceptable geometry. Because of proteolysis, 58 of 419 amino acids of the canavalin polypeptide are not visible in the electron density map. The canavalin subunit is composed of two extremely similar structural domains that reflect the tandem duplication observed in the cDNA and in the amino acid sequence. Each domain consists of two elements, a compact, eight-stranded beta-barrel having the "Swiss roll" topology and an extended loop containing several short alpha-helices. The root mean square deviation between 84 pairs of corresponding C alpha atoms making up the strands of the two beta-barrels in a subunit is 0.78 A, and for 112 pairs of structurally equivalent C alpha atoms of the two domains the deviation is 1.37 A. The interface between domains arises from the apposition of broad hydrophobic surfaces formed by side chains originating from one side of the beta-barrels, supplemented by at least four salt bridges. The interfaces between subunits in the trimer are supplied by the extended loop elements. These interfaces are also composed primarily of hydrophobic residues supplemented by six salt bridges. The canavalin subunits have dimensions about 40 x 40 x 86 A, and the oligomer is a disk-shaped molecule about 88 A in diameter with a thickness of about 40 A. The distribution of domains lends a high degree of pseudo-32-point group symmetry to the molecule. There is a large channel of 18 A diameter, lined predominantly by hydrophilic and charged amino acids, running through the molecule along the 3-fold axis. The majority of residues conserved between domains and among vicilins occur at the interface between subunits but appear otherwise arbitrarily distributed within the subunit, although predominantly on its exterior.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-1112813, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-1180565, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-1628747, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-16662638, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-16663793, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-17810339, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-2185018, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-2297559, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-2488475, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-3013879, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-3062181, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-3841179, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-4079790, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-4882249, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-7055627, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-8310055, http://linkedlifedata.com/resource/pubmed/commentcorrection/8310056-875032
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
101
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
729-44
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis).
pubmed:affiliation
Department of Biochemistry, University of California, Riverside 92521.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.