Campeotto Ivan, Carr Stephen B, Trinh Chi H, Nelson Adam S, Berry Alan, Phillips Simon E V, Pearson Arwen R
Astbury Centre for Structural Molecular Biology, University of Leeds, England.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt 11):1088-90. doi: 10.1107/S1744309109037403. Epub 2009 Oct 24.
The structure of a mutant variant of Escherichia coli N-acetyl-d-neuraminic acid lyase (NAL), E192N, in complex with pyruvate has been determined in a new crystal form. It crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 78.3, b = 108.5, c = 148.3 angstrom. Pyruvate has been trapped in the active site as a Schiff base with the catalytic lysine (Lys165) without the need for reduction. Unlike the previously published crystallization conditions for the wild-type enzyme, in which a mother-liquor-derived sulfate ion is strongly bound in the catalytic pocket, the low-salt conditions described here will facilitate the determination of further E. coli NAL structures in complex with other activesite ligands.
已通过一种新的晶体形式确定了大肠杆菌N-乙酰-D-神经氨酸裂解酶（NAL）的突变变体E192N与丙酮酸复合物的结构。它在空间群P2(1)2(1)2(1)中结晶，晶胞参数a = 78.3、b = 108.5、c = 148.3埃。丙酮酸作为席夫碱与催化赖氨酸（Lys165）被困在活性位点，无需还原。与先前公布的野生型酶的结晶条件不同，在先前条件下母液衍生的硫酸根离子强烈结合在催化口袋中，此处描述的低盐条件将有助于确定大肠杆菌NAL与其他活性位点配体复合物的更多结构。
