New York SGX Research Center for Structural Genomics, Eli Lilly and Company, Lilly Biotechnology Center, San Diego, California 92121, USA.
Proteins. 2010 Nov 1;78(14):3056-62. doi: 10.1002/prot.22829.
The X-ray structure of a putative BenF-like (gene name: PFL1329) protein from (PflBenF) has been determined at 2.6Å resolution. X-ray crystallography revealed a canonical 18-stranded β-barrel fold that forms a central pore with a diameter of ∼4.6Å, which is consistent with the size and physicochemical properties of the presumed aromatic acid substrate, benzoate. Detailed comparisons with the previously-determined structure of OpdK, a vanillate influx channel, revealed an arginine-rich aromatic acid selectivity filter of nearly identical structure composed of seven highly conserved residues Arg∼Asp∼Arg∼Arg∼Ser∼Asp∼Arg (R∼D∼R∼R∼S∼D∼R sequence motif, where ∼ denotes intervening residues) that define the narrowest part of the pore.
来自 （PflBenF）的假定 BenF 样（基因名称：PFL1329）蛋白的 X 射线结构已在 2.6Å 分辨率下确定。X 射线晶体学揭示了一个典型的 18 股β桶折叠，形成一个直径约为 4.6Å 的中央孔，这与假定的芳香酸底物苯甲酸的大小和物理化学性质一致。与先前确定的香草酸盐流入通道 OpdK 的结构进行详细比较，发现了一个由七个高度保守的残基 Arg∼Asp∼Arg∼Arg∼Ser∼Asp∼Arg（R∼D∼R∼R∼S∼D∼R 序列基序组成的富含精氨酸的芳香酸选择性过滤器，几乎相同的结构，其中 ∼ 表示间隔残基），定义了孔的最窄部分。
