S. PYOGENES IMPDH IS A TETRAMER WITH ITS FOUR SUBUNITS RELATED BY A CRYSTALLOGRAPHIC FOURFOLD AXIS. EACH MONOMER HAS A TWO-DOMAIN STRUCTURE: A CATALYTIC DOMAIN (AMINO ACID RESIDUES 2-92 AND 224-492) FORMING THE INTERIOR CORE OF THE ACTIVE TETRAMERIC ENZYME AND A CBS DIMER DOMAIN (RESIDUES 93-223) PROJECTING OUTWARD FROM THE CORNERS OF THE SQUARE. THE CBS DESIGNATION ARISES FROM THE ORIGINAL IDENTIFICATION OF THIS FOLDING MOTIF IN THE ENZYME CYSTATHIONINE-"BETA"-SYNTHASE [BATEMAN, A. (1997) TRENDS BIOCHEM. SCI. 22, 12-13]. THE CBS DIMER DOMAIN, FOUND IN IMPDH PROTEINS FROM ALL THREE KINGDOMS, IS COMPOSED OF TWO CBS MOTIFS RELATED BY APPROXIMATE TWOFOLD SYMMETRY (RMS DEVIATIONS BETWEEN ALPHA CARBON ATOMS: 2.7 ANGSTROMS). EACH CBS MOTIF HAS THE CHARACTERISTIC SHEET/HELIX/SHEET/SHEET/HELIX TOPOLOGY. THIS IS THE FIRST REPORTED COMPLETE STRUCTURE OF A CBS DIMER DOMAIN, A FOLDING MOTIF PROPOSED TO ACT AS A REGULATORY ELEMENT SINCE MUTATIONS LEAD TO THE HUMAN DISEASE HOMOCYSTINURIA. EACH IPMDH MONOMER CONTAINS IMP IN THE CATALYTIC SITE. THIS SUBSTRATE IS NOT COVALENTLY BOUND TO THE ACTIVE SITE CYS310 SUGGESTING THAT IMP DOES NOT FORM A COVALENT BOND IN THE ABSENCE OF NAD.
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Components
#1: Protein
INOSINEMONOPHOSPHATEDEHYDROGENASE
Mass: 53228.352 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, CBS DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus pyogenes (bacteria) / Production host: Streptococcus pyogenes (bacteria) / Strain (production host): ESCHERICHIA COLI / References: UniProt: P0C0H6, IMP dehydrogenase
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