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

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

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

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

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

Authors

J C Génovésio-Taverne¹, U Sauder, R A Pauptit, J N Jansonius, B Erni

Affiliation

¹ Department of Structural Biology, University of Basel, Switzerland.

PMID: 2258928
DOI: 10.1016/0022-2836(90)90379-Z

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Crystallization
Escherichia coli / enzymology*
Peptide Fragments / chemistry
Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry*
Phosphorylation
X-Ray Diffraction

Substances

Bacterial Proteins
Peptide Fragments
Phosphoenolpyruvate Sugar Phosphotransferase System
phosphoenolpyruvate-mannose phosphotransferase