Linked Life Data

1453466

Source:http://linkedlifedata.com/resource/pubmed/id/1453466

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-12-31
pubmed:abstractText
The structure of wild-type bacteriophage T4 glutaredoxin (earlier called thioredoxin) in its oxidized form has been refined in a monoclinic crystal form at 2.0 A resolution to a crystallographic R-factor of 0.209. A mutant T4 glutaredoxin gives orthorhombic crystals of better quality. The structure of this mutant has been solved by molecular replacement methods and refined at 1.45 A to an R-value of 0.175. In this mutant glutaredoxin, the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, to mimic that of Escherichia coli thioredoxin. The main-chain conformation of the wild-type protein is similar in the two independently determined molecules in the asymmetric unit of the monoclinic crystals. On the other hand, side-chain conformations differ considerably between the two molecules due to heterologous packing interactions in the crystals. The structure of the mutant protein is very similar to the wild-type protein, except at mutated positions and at parts involved in crystal contacts. The active site disulfide bridge between Cys14 and Cys17 is located at the first turn of helix alpha 1. The torsion angles of these residues are similar to those of Escherichia coli thioredoxin. The torsion angle around the S-S bond is smaller than that normally observed for disulfides: 58 degrees, 67 degrees and 67 degrees for wild-type glutaredoxin molecule A and B and mutant glutaredoxin, respectively. Each sulfur atom of the disulfide cysteines in T4 glutaredoxin forms a hydrogen bond to one main-chain nitrogen atom. The active site is shielded from solvent on one side by the beta-carbon atoms of the cysteine residues plus side-chains of residues 7, 9, 21 and 33. From the opposite side, there is a cleft where the sulfur atom of Cys14 is accessible and can be attacked by a nucleophilic thiolate ion in the initial step of the reduction reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
228
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
596-618
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:1453466-Amino Acid Sequence, pubmed-meshheading:1453466-Bacteriophage T4, pubmed-meshheading:1453466-Binding Sites, pubmed-meshheading:1453466-Computer Simulation, pubmed-meshheading:1453466-Disulfides, pubmed-meshheading:1453466-Escherichia coli, pubmed-meshheading:1453466-Glutaredoxins, pubmed-meshheading:1453466-Hydrogen Bonding, pubmed-meshheading:1453466-Metals, pubmed-meshheading:1453466-Molecular Sequence Data, pubmed-meshheading:1453466-Mutation, pubmed-meshheading:1453466-Oxidation-Reduction, pubmed-meshheading:1453466-Oxidoreductases, pubmed-meshheading:1453466-Protein Conformation, pubmed-meshheading:1453466-Proteins, pubmed-meshheading:1453466-Solvents, pubmed-meshheading:1453466-Temperature, pubmed-meshheading:1453466-Thioredoxins, pubmed-meshheading:1453466-Viral Proteins, pubmed-meshheading:1453466-X-Ray Diffraction
pubmed:year
1992
pubmed:articleTitle
Structure of oxidized bacteriophage T4 glutaredoxin (thioredoxin). Refinement of native and mutant proteins.
pubmed:affiliation
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't