Crystal structure of putative monooxygenase (YP_193413.1) from Lactobacillus acidophilus NCFM at 1.55 A resolution

Joint Center for Structural Genomics (JCSG)

ADJUSTABLE FOCUSING MIRRORS IN K-B GEOMETRY

G(MSE)DETPIFKIKKLTIAENDRSEYIRYAEKN(MSE)HDSIPAEEGTLLIGSGHDDAHGEDNYEIEVFRNKGAEDLHI
AGSHADDFVETVNKIATKQKVIDLHPEVITTKAQRALNSYADNFV(MSE)RLIKVEVKDADAEKFSHAVKKE(MSE)TTS
(MSE)ASEPG(MSE)EI(MSE)(MSE)SGTNIDNPNEWYFIEVYANDEAYDIHVKTPHYKEYIEETDG(MSE)VKSRDVK
TLVRDTLATQGAIVLD

GMDETPIFKIKKLTIAENDRSEYIRYAEKNMHDSIPAEEGTLLIGSGHDDAHGEDNYEIEVFRNKGAEDLHIAGSHADDF
VETVNKIATKQKVIDLHPEVITTKAQRALNSYADNFVMRLIKVEVKDADAEKFSHAVKKEMTTSMASEPGMEIMMSGTNI
DNPNEWYFIEVYANDEAYDIHVKTPHYKEYIEETDGMVKSRDVKTLVRDTLATQGAIVLD

THE STATISTICS REPORTED IN THE REMARK 200 STATEMENTS ABOVE WERE COMPUTED WITH THE FRIEDEL PAIRS KEPT SEPARATE.

0.2000M Ca(OAc)2, 20.0000% PEG-8000, 0.1M MES pH 6.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORDS CONTAIN 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. ACT MOLECULES FROM THE CRYSTALLIZATION SOLUTION ARE MODELED.

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

YP_193413.1, putative monooxygenase, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, Unknown function, OXIDOREDUCTASE

MDETPIFKIKKLTIAENDRSEYIRYAEKNMHDSIPAEEGTLLIGSGHDDAHGEDNYEIEVFRNKGAEDLHIAGSHADDFV
ETVNKIATKQKVIDLHPEVITTKAQRALNSYADNFVMRLIKVEVKDADAEKFSHAVKKEMTTSMASEPGMEIMMSGTNID
NPNEWYFIEVYANDEAYDIHVKTPHYKEYIEETDGMVKSRDVKTLVRDTLATQGAIVLD