2plh
From Proteopedia
|
STRUCTURE OF ALPHA-1-PUROTHIONIN AT ROOM TEMPERATURE AND 2.8 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of alpha(1)-purothionin (alpha(1)-PT), a, wheat-germ protein and a basic lytic toxin, was previously solved by, molecular-replacement methods using an energy-minimized predicted model, and refined to an R-factor of 21.6% [Teeter, Ma, Rao & Whitlow (1990)., Proteins Struct. Funct. Genet. 8, 118-1321. Some deficiencies of the model, motivated us to revisit the structure and to continue the refinement. Here, we report a significantly improved structure refined to an R-factor of, 15.5% with excellent geometry. The refinement of this relatively low, resolution structure ( approximately 2.8 A) is well suited to test the, limitations of classical methods of refinement and to address the problem, of overfitting, The final structure contains 434 atoms including 330, protein atoms, 70 waters, three acetates, two glycerols, one sec-butanol, and one phosphate. The key solute molecules (acetate ion and phosphate, ion) play a crucial role in the lattice formation. Phosphate and glycerol, found in the structure may be important for biological activity of the, toxins.
About this Structure
2PLH is a Single protein structure of sequence from Triticum aestivum with ACT, PO4, SBT and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Refinement of purothionins reveals solute particles important for lattice formation and toxicity. Part 1: alpha1-purothionin revisited., Rao U, Stec B, Teeter MM, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):904-13. PMID:15299760
Page seeded by OCA on Wed Nov 21 13:35:01 2007
Categories: Single protein | Triticum aestivum | Rao, U. | Stec, B. | Teeter, M.M. | ACT | GOL | PO4 | SBT | Disulfide rich | Membrane active
