大肠杆菌甘露糖通透酶磷酸化亚基N端结构域的结晶及初步X射线衍射研究

Crystallization and preliminary X-ray diffraction studies of the N-terminal domain of the phosphorylating subunit of mannose permease from Escherichia coli.

作者信息

Génovésio-Taverne J C, Sauder U, Pauptit R A, Jansonius J N, Erni B

机构信息

Department of Structural Biology, University of Basel, Switzerland.

出版信息

J Mol Biol. 1990 Dec 5;216(3):515-7. doi: 10.1016/0022-2836(90)90379-Z.

DOI:10.1016/0022-2836(90)90379-Z

PMID:2258928

Abstract

Mannose permease is a constitutive component of the phosphotransferase system in Escherichia coli. This complex consists of two transmembrane subunits (II-PMan, Mr = 28,000 and II-MMan, Mr = 31,000) and a hydrophilic subunit (IIIMan). IIIMan functions as a phosphorylating enzyme and exists as a soluble homo-dimer of Mr = 70,000 in the cytosol. The N-terminal domain (P13) of IIIMan contains a phosphorylation site and the interface for dimerization. P13 has been crystallized in two different forms: type I, orthorhombic, space group C222 with a = 98.7 A, b = 106.5 A and c = 57.4 A, and type II, monoclinic, space group P2(1), with a = 54.4 A, b = 100.5 A, c = 58.1 A and beta = 90.5 degrees. Both types of crystal are suitable for X-ray diffraction studies.

摘要

甘露糖通透酶是大肠杆菌磷酸转移酶系统的一个组成成分。这个复合体由两个跨膜亚基（II-PMan，分子量28,000；II-MMan，分子量31,000）和一个亲水性亚基（IIIMan）组成。IIIMan作为一种磷酸化酶发挥作用，在胞质溶胶中以分子量70,000的可溶性同型二聚体形式存在。IIIMan的N端结构域（P13）包含一个磷酸化位点和二聚化界面。P13已以两种不同形式结晶：I型，正交晶系，空间群C222，a = 98.7 Å，b = 106.5 Å，c = 57.4 Å；II型，单斜晶系，空间群P2(1)，a = 54.4 Å，b = 100.5 Å，c = 58.1 Å，β = 90.5°。两种晶体都适合进行X射线衍射研究。