Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein.

Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein. Research Abstract Details 

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Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein. Abstract Text:

K A Stauffer,A Hoenger,A Engel,

We have reconstituted Escherichia coli maltoporin into phospholipid membranes at low lipid-to-protein ratios to produce two-dimensional crystals of this membrane protein. Electron microscopy of negatively stained membranes showed three different types of arrays, two of them hexagonal and the third rectangular, all diffracting to approximately (2 nm)-1. Furthermore, we have core-constituted maltoporin with the maltose-binding protein from E. coli, a soluble periplasmic protein that has been proposed to interact with maltoporin. One of the hexagonal arrays was found to bind maltose-binding protein molecules in a regular way, while the maltose-binding protein binding sites were not accessible in the other crystal forms. Difference maps from averaged decorated arrays and undecorated controls showed three symmetry-related maltose-binding protein binding sites per maltoporin trimer, of which not more than one is likely to be occupied at a given time. Using multivariate statistical analysis to select similar unit cells of the decorated maltoporin array, we have obtained a map showing the rough outline of a maltose-binding protein molecule interacting with the pore formed by a maltoporin trimer.

Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein. Publishing Authors By Initials

KA Stauffer,A Hoenger,A Engel,

For similar proteins: membrane proteins: receptors, cell surface: receptors, virus research abstracts see: proteins: membrane proteins: receptors, cell surface: receptors, virus research

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Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of molecular biology

VOLUME: 223

Page Numbers: 1155-65

Journal Abbreviation: J. Mol. Biol.

ISSN: 0022-2836

DAY: 20

MONTH: Feb

YEAR: 1992

Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein. Information

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LANGUAGE: eng

NlmUniqueID: 2985088

Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein. Keywords Mesh Terms:

KEYWORDS: Receptors, Virus

MESH TERMS: ultrastructure

Chemical & Substance for Abstract: Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein. Information

Substance Name: maltose-binding protein

Registry Number: 0

Grant and Affiliation Information for Two-dimensional crystals of Escherichia coli maltoporin and their interaction with the maltose-binding protein.

AFFILIATION: Department of Microbiology, University of Basel, Switzerland.

Country: ENGLAND

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MEDLINETA: J Mol Biol

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