Crystal structure of a ph domain containing bacterial protein (exig_2160) from exiguobacterium sibiricum 255-15 at 2.42 A resolution

Joint Center for Structural Genomics (JCSG)

Bacterial pleckstrin homology domains: a prokaryotic origin for the PH domain.

GSDIGQVIHPDDFDKAAADDYVLHEDGEKIYFLIKSKTDEYCFTNLALVHLDGESAVSSKRVLYRYPYAHYPIRHV
(MSE)FETAGTVDLDVEIKFEIGGKHYSIDVDKKQLEHVKDLYKALLAIAEKQYEGQK(MSE)LEFANSSLNHSVTILGG
LRQGD(MSE)NVPQTFKDLSQESFDWLQGHYYKWNQKDFGSFYEKYINN

GSDIGQVIHPDDFDKAAADDYVLHEDGEKIYFLIKSKTDEYCFTNLALVHLDGESAVSSKRVLYRYPYAHYPIRHVMFET
AGTVDLDVEIKFEIGGKHYSIDVDKKQLEHVKDLYKALLAIAEKQYEGQKMLEFANSSLNHSVTILGGLRQGDMNVPQTF
KDLSQESFDWLQGHYYKWNQKDFGSFYEKYINN

NANODROP, 10.0% PEG 6000, 0.1M Bicine pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K

SEQUENCE
THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

REMARK 999 SEQUENCE: THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY
OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO
PARTIAL S-MET INCORPORATION.
4. DENSITIES FOR THE FOLLOWING REGIONS ARE POOR FOR
ALL CHAINS: 64-71, 158-164.

Pleckstrin-homology domain, structural genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, unknown function

SDIGQVIHPDDFDKAAADDYVLHEDGEKIYFLIKSKTDEYCFTNLALVHLDGESAVSSKRVLYRYPYAHYPIRHVMFETA
GTVDLDVEIKFEIGGKHYSIDVDKKQLEHVKDLYKALLAIAEKQYEGQKMLEFANSSLNHSVTILGGLRQGDMNVPQTFK
DLSQESFDWLQGHYYKWNQKDFGSFYEKYINN