Crystallization (Comment) | Organism |
---|---|
crystal structure of the enzyme bound to the product UDP-N-acetyl-alpha-D-mannosaminuronate by X-ray diffraction to resolution of 1.55 A. Crystal structures reveal a tight dimeric polymer chains with product-bound in all the structures. The catalytic residues Cys258 and Lys204 are conserved. The Cys258 acts as catalytic nucleophile and Lys204 as acid/base catalyst. The product directly interacts with residues Arg211, Thr249, Arg244, Gly255, Arg289, Lys319 and Arg398. The SeMet-substituted enzyme is crystallized using microbatch sitting method under reservoir solution condition 10% (w/v) PEG 8000, 8% (v/v) ethylene glycol and 0.1 M HEPES, pH 7.5 | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
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Pyrococcus horikoshii | - |
- |
- |
Pyrococcus horikoshii OT-3 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus horikoshii |
Subunits | Comment | Organism |
---|---|---|
dimer | monomers aggregate to dimeric form with major interactions from oligomerization domain residues | Pyrococcus horikoshii |
Synonyms | Comment | Organism |
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UDP-D-ManNAcDH | - |
Pyrococcus horikoshii |