RECOMBINANT SERINE HYDROXYMETHYLTRANSFERASE (MOUSE)

Structure of a murine cytoplasmic serine hydroxymethyltransferase quinonoid ternary complex: evidence for asymmetric obligate dimers.

MADRDATLWASHEK(MSE)LSQPLKDSDAEVYSIIKKESNRQRVGLELIASENFASRAVLEALGSSLNNKYSEGYPGQRY
YGGTEFIDELE(MSE)LCQKRALQAYHLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRI(MSE)GLDLPDGGHLTHGF
(MSE)TDKKKISATSIFFES(MSE)PYKVYPETGYINYDQLEENASLFHPKLIIAGTSCYSRNLDYARLRKIADDNGAYL
(MSE)AD(MSE)AHISGLVAAGVVPSPFEHCHVVTTTTHKTLRGCRAG(MSE)IFYRKGVRSVDPKTGKETYYELESLIN
SAVFPGLQGGPHNHAIAGVAVALKQA(MSE)TTEFKIYQLQVLANCRALSDALTELGYKIVTGGSDNHLIL(MSE)DLRS
KGTDGGRAEKVLEACSIACNKNTCPGDKSALRPSGLRLGTPALTSRGLLEEDFQKVAHFIHRGIELTLQIQSH(MSE)AT
KATLKEFKEKLAGDEKIQSAVATLREEVENFASNFSLPGLPDF

MADRDATLWASHEKMLSQPLKDSDAEVYSIIKKESNRQRVGLELIASENFASRAVLEALGSSLNNKYSEGYPGQRYYGGT
EFIDELEMLCQKRALQAYHLDPQCWGVNVQPYSGSPANFAVYTALVEPHGRIMGLDLPDGGHLTHGFMTDKKKISATSIF
FESMPYKVYPETGYINYDQLEENASLFHPKLIIAGTSCYSRNLDYARLRKIADDNGAYLMADMAHISGLVAAGVVPSPFE
HCHVVTTTTHKTLRGCRAGMIFYRKGVRSVDPKTGKETYYELESLINSAVFPGLQGGPHNHAIAGVAVALKQAMTTEFKI
YQLQVLANCRALSDALTELGYKIVTGGSDNHLILMDLRSKGTDGGRAEKVLEACSIACNKNTCPGDKSALRPSGLRLGTP
ALTSRGLLEEDFQKVAHFIHRGIELTLQIQSHMATKATLKEFKEKLAGDEKIQSAVATLREEVENFASNFSLPGLPDF

RESOLUTION RANGES 3.96-3.84 AND 3.72-3.64 A EXCLUDED FROM PROCESSING BECAUSE OF ICE RINGS.

8% PEG 8000, 6% ETHYLENE GLYCOL, 0.1 M HEPES, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K

RABBIT SHMT (1CJ0) DIMER, WITH 2 PLP COFACTORS. EACH MONOMER WAS MODIFIED BY: OMISSION OF RESIDUES 269-287 (IN THE HUMAN SHMT NUMBERING SCHEME; LABELED 241-250 IN THE 1CJ0 ENTRY), CONVERSION OF ALL MET RESIDUES TO SEMET, AND CONVERSION TO ALANINE OF RESIDUES WHICH DIFFER BETWEEN RABBIT AND MOUSE, I.E. RESIDUES 16, 20, 35, 68, 88, 94, 175, 177, 182, 185, 191, 220, 237, 322, 326, 329, 332, 343, 361, 416, 433, 437-439, 441-442, 458, 460, 463, 467, 471, 475, AND 477 IN THE HUMAN SHMT NUMBERING SCHEME.

FOR EACH GROUP, RESTRAINTS WERE APPLIED AMONG THE 4 CHAINS A, B, C, AND D. GROUP 1: MAIN CHAIN ATOMS FOR RESIDUES 15-77, 84-144, 162-256, 259-270, 287-294, 300-382, 400-435, AND 459-479

RECOMBINANT SERINE HYDROXYMETHYLTRANSFERASE (MOUSE) (E.C.2.1.2.1)

SERINE-GLYCINE CONVERSION, PYRIDOXAL 5'-PHOSPHATE, TETRAHYDROFOLATE, ASYMMETRIC DIMER, TRANSFERASE

ACTIVE SITE CONTAINING GLY-PLP COMPLEX AND THF INHIBITOR. SITE RESIDUES ARE FROM CHAINS A AND B.

ACTIVE SITE CONTAINING GLY-PLP COMPLEX AND THF INHIBITOR. SITE RESIDUES ARE FROM CHAINS B AND A.

ACTIVE SITE CONTAINING GLY-PLP COMPLEX ONLY. SITE RESIDUES ARE FROM CHAINS C AND D.

ACTIVE SITE CONTAINING GLY-PLP COMPLEX AND THF INHIBITOR. SITE RESIDUES ARE FROM CHAINS D AND C.