幽门螺杆菌中性粒细胞激活蛋白（HP-NAP）的一种新晶格结构。
A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP).
作者信息
Tsuruta Osamu, Yokoyama Hideshi, Fujii Satoshi
机构信息
School of Pharmaceutical Sciences, University of Shizuoka, Suruga-ku, Shizuoka-shi, Shizuoka, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):134-40. doi: 10.1107/S1744309111052675. Epub 2012 Jan 25.
Abstract
A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP) has been determined in two forms: the native state (Apo) at 2.20 Å resolution and an iron-loaded form (Fe-load) at 2.50 Å resolution. The highly solvated packing of the dodecameric shell is suitable for crystallographic study of the metal ion-uptake pathway. Like other bacterioferritins, HP-NAP forms a spherical dodecamer with 23 symmetry including two kinds of channels. Iron loading causes a series of conformational changes of amino-acid residues (Trp26, Asp52 and Glu56) at the ferroxidase centre.
摘要
幽门螺杆菌中性粒细胞激活蛋白（HP-NAP）的一种新晶格结构已被确定为两种形式：分辨率为2.20 Å的天然状态（无铁状态）和分辨率为2.50 Å的铁负载形式。十二聚体外壳的高度溶剂化堆积适合于金属离子摄取途径的晶体学研究。与其他细菌铁蛋白一样，HP-NAP形成具有23对称性的球形十二聚体，包括两种通道。铁负载会导致铁氧化酶中心的氨基酸残基（Trp26、Asp52和Glu56）发生一系列构象变化。
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