3ngg
X-ray Structure of OmwaprinX-ray Structure of Omwaprin
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 50-residue snake venom protein L-omwaprin and its enantiomer D-omwaprin were prepared by total chemical synthesis. Radial diffusion assays were performed against Bacillus megaterium and Bacillus anthracis; both L-omwaprin and D-omwaprin showed anti-bacterial activity against B. megaterium. The native protein enantiomer, made of L- amino acids, failed to crystallize readily. However, when a racemic mixture containing equal amounts of L-omwaprin and D-omwaprin was used, diffraction quality crystals were obtained. The racemic protein sample crystallized in the centrosymmetric space group P2(1)/c and its structure was determined at atomic resolution (1.33 A) by a combination of Patterson and direct methods based on the strong scattering from the sulfur atoms in the eight cysteine residues per protein. Racemic crystallography once again proved to be a valuable method for obtaining crystals of recalcitrant proteins, and for determining high resolution X-ray structures by direct methods. Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography.,Banigan JR, Mandal K, Sawaya MR, Thammavongsa V, Hendrickx AP, Schneewind O, Yeates TO, H Kent SB Protein Sci. 2010 Jul 28. PMID:20669184[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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