Crystal structure of a putative lipoprotein (ACTODO_00931) from Actinomyces odontolyticus ATCC 17982 at 2.35 A resolution

Joint Center for Structural Genomics (JCSG)

Crystal structure of a hypothetical protein ACTODO_00931 (hypothetical protein ACTODO_00931, SP17422A, P_02044074.1) from Actinomyces odontolyticus ATCC 17982 at 2.35 A resolution

GSSSDVVTLTVGATPSPHAKILTYINDNLAADAGIKLDIVEYTDYVQPNTALNDGDLDANFYQTVPYLENAEKQFGYNFE
AGEGIHLEPLGVFSNKHKSLDELPDGGTIGIISDTANQSRALELLATQGLVSIPEGDGDVNINTVTKLKNFDFREVEGPQ
LVRSLDDFDYAVINGNFAQEGGKTISGDALVVESPVDNPAVNVLVWKGDSKKVDAIAKLEKLLHSDEVKQYIEKTWSDGS
VIPAF

20.00% polyethylene glycol 1000, 0.1M TRIS pH 7.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K

THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 34-277 OF THE TARGET SEQUENCE.

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 5. A SELENO-METHIONINE AMINO ACID HAS BEEN MODELED AS A LIGAND BASED ON THE ELECTRON DENSITY. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. ANOMALOUS DIFFERENCE FOURIERS MAP SUPPORTS THE MODELING OF MET AS MSE. 6. PEG FRAGMENTS (PE4, PG4) FROM THE CRYSTALLIZATION/CRYOPROTECTION SOLUTIONS ARE MODELED.

Tom Terwilliger, Frank DiMaio, Randy Read, David Baker

CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.

MEMBRANE LIPOPROTEIN, L-METHIONINE BINDING PROTEIN, NLPA lipoprotein, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-BIOLOGY, METHIONINE-BINDING PROTEIN