3NGG

X-ray Structure of Omwaprin

Summary for 3NGG

• Entry DOI: 10.2210/pdb3ngg/pdb
• Descriptor: Omwaprin-a (2 entities in total)
• Functional Keywords: venom protein, racemic protein crystallography, direct methods, antibiotic
• Biological source: Oxyuranus microlepidotus (Inland taipan)
• Cellular location: Secreted: P83952
• Total number of polymer chains: 2
• Total formula weight: 11243.13

Authors

Banigan, J.R.,Mandal, K.,Sawaya, M.R.,Thammavongsa, V.,Hendrickx, A.P.A.,Schneewind, O.,Yeates, T.O.,Kent, S.B.H. (deposition date: 2010-06-11, release date: 2010-09-08, Last modification date: 2024-10-09)

Primary citation

Banigan, J.R.,Mandal, K.,Sawaya, M.R.,Thammavongsa, V.,Hendrickx, A.P.,Schneewind, O.,Yeates, T.O.,Kent, S.B.
Determination of the X-ray structure of the snake venom protein omwaprin by total chemical synthesis and racemic protein crystallography.
Protein Sci., 19:1840-1849, 2010

PubMed Abstract: The 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- and D-omwaprin showed antibacterial 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- 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.

PubMed: 20669184
DOI: 10.1002/pro.468

Experimental method

X-RAY DIFFRACTION (1.33 Å)