High-resolution diffraction from crystals of a membrane-protein complex: bacterial outer membrane protein OmpC complexed with the antibacterial eukaryotic protein lactoferrin

Baalaji, N. Sundara ; Acharya, K. Ravi. ; Singh, T. P. ; Krishnaswamy, S. (2005) High-resolution diffraction from crystals of a membrane-protein complex: bacterial outer membrane protein OmpC complexed with the antibacterial eukaryotic protein lactoferrin Acta Crystallographica Section F, 61 (8). pp. 773-775. ISSN 1744-3091

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Official URL: http://onlinelibrary.wiley.com/doi/10.1107/S174430...

Related URL: http://dx.doi.org/10.1107/S1744309105022086

Abstract

Crystals of the complex formed between the outer membrane protein OmpC from Escherichia coli and the eukaryotic antibacterial protein lactoferrin from Camelus dromedarius (camel) have been obtained using a detergent environment. Initial data processing suggests that the crystals belong to the hexagonal space group P6, with unit-cell parameters a = b = 116.3, c = 152.4 Å,α =β= 90, γ= 120°. This indicated a Matthews coefficient (VM) of 3.3 Å3 Da-1, corresponding to a possible molecular complex involving four molecules of lactoferrin and two porin trimers in the unit cell (4832 amino acids; 533.8 kDa) with 63% solvent content. A complete set of diffraction data was collected to 3Åresolution at 100 K. Structure determination by molecular replacement is in progress. Structural study of this first surface-exposed membrane-protein complex with an antibacterial protein will provide insights into the mechanism of action of OmpC as well as lactoferrin.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
Keywords:OmpC; Lactoferrin; Detergents; Antibacterial Proteins; Membrane-Protein Complexes
ID Code:49178
Deposited On:19 Jul 2011 07:13
Last Modified:19 Jul 2011 07:13

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