Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1990-12-21
|
pubmed:abstractText |
Alpha 1-Purothionin (alpha 1-P), a wheatgerm protein and lytic toxin, has a secondary and tertiary structure similar to that of crambin as revealed by CD and NMR studies. alpha 1-P crystallizes in the tetragonal space group 1422 with unit cell dimensions: a = b = 53.59 and c = 69.79 A. X-ray diffraction data have been measured to 2.5 A Bragg spacing. The crystal structure has been determined by molecular replacement methods, using an energy-minimized alpha 1-P model structure derived from crambin (Whitlow and Teeter: Journal of Biomolecular Structure and Dynamics 2:831-848, 1985, Journal of the American Chemical Society 108:7163-7172, 1986). The energy-minimized model gives a slightly cleaner rotation solution and better refinement against the x-ray data than do the crambin or unminimized alpha 1-P structures. The final crystallographic residual with the data in the 10-2.5 A resolution range is 0.216. The refined alpha 1-P structure has a backbone rms difference of 0.74 A from crambin and 0.55 A from the energy-minimized alpha 1-P model. A low resolution NMR model of alpha 1-P calculated from metric matrix distance geometry and restrained molecular dynamics differs from crambin's backbone by 2.3 A rms deviation (Clore et al.: EMBO Journal 5:2729-2735, 1986). Backbone dihedral angles for our predicted model differ from the refined alpha 1-P structure in only one region (at a turn where there is a deletion relative to crambin). The NMR model had differences in four regions.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antimicrobial Cationic Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/crambin protein, Crambe abyssinica,
http://linkedlifedata.com/resource/pubmed/chemical/purothionin
|
pubmed:status |
MEDLINE
|
pubmed:issn |
0887-3585
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
8
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
118-32
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:2235992-Antimicrobial Cationic Peptides,
pubmed-meshheading:2235992-Computer Simulation,
pubmed-meshheading:2235992-Magnetic Resonance Spectroscopy,
pubmed-meshheading:2235992-Models, Molecular,
pubmed-meshheading:2235992-Plant Proteins,
pubmed-meshheading:2235992-Protein Conformation,
pubmed-meshheading:2235992-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2235992-Stereoisomerism,
pubmed-meshheading:2235992-Structure-Activity Relationship,
pubmed-meshheading:2235992-X-Ray Diffraction
|
pubmed:year |
1990
|
pubmed:articleTitle |
Crystal structure of a protein-toxin alpha 1-purothionin at 2.5A and a comparison with predicted models.
|
pubmed:affiliation |
Department of Chemistry, Boston College, Chestnut Hill, Massachusetts 02167.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|