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Literature summary for 2.7.7.9 extracted from

  • Thoden, J.B.; Holden, H.M.
    Active site geometry of glucose-1-phosphate uridylyltransferase (2007), Protein Sci., 16, 1379-1388.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Corynebacterium glutamicum

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with both Mg2+ and UDP-glucose. Residues involved in anchoring the ligand to the active site include the polypeptide chain backbone atoms of Ala20, Gly21, Gly117, Gly180, and Ala214, and the side chains of Glu36, Gln112, Asp143, Glu201, and Lys202. Two magnesium ions are coordinated to the UDP-glucose. An alpha- and a beta-phosphoryl oxygen, three waters, and the side chain of Asp142 ligate the first Mg2+ ion, whereas the second ion is coordinated by an alpha-phosphoryl oxygen and five waters Corynebacterium glutamicum
in presence of both magnesium and UDP-glucose. Residues anchoring the ligand to the acitve site include polypepetide backbone atoms of A20, G21, G117, G180 and A214 and side chain residues of E36, Q112, D143, E201, and K202. Two magnesium ions coordinate to UDP-glucose Corynebacterium glutamicum

Metals/Ions

Metals/Ions Comment Organism Structure
Magnesium crystallization data, two magnesium ions coordinate to UDP-glucose. Magnesium is involved in catalytic mechanism Corynebacterium glutamicum

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
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Purification (Commentary)

Purification (Comment) Organism
recombinant protein Corynebacterium glutamicum