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EC Number
Crystallization (Commentary)
Reference
3.4.24.B16
crystal structures of active LasA as a complex with tartrate and in the uncomplexed form, to 1.28 A resolution. The overall fold resembles that of the other M23 family members, the LasA active site is less constricted and utilizes a different set of metal ligands. The active site of uncomplexed LasA contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules. Manual docking study of the pentapeptide Gly-Gly-Phe-Gly-Gly in the active site so that the carbonyl oxygen of the scissile peptide occupies the approximate position of Tyr151-bound tartrate oxygen O1 and the P2 and P1 glycines follow the path of the tartrate carbon skeleton
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