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

N Sundara Baalaji·K Ravi Acharya·T P Singh·S Krishnaswamy
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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 A, alpha = beta = 90, gamma = 120 degrees. This indicated a Matthews coefficient (VM) of 3.3 A3 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 3 A resolution 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.

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AnimalsAnti-Bacterial AgentsBacterial Outer Membrane ProteinsCamelusCrystallizationDiffusionEscherichia coliLactoferrinPorinsX-Ray DiffractionJournal ArticleResearch Support, Non-U.S. Gov't

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N Sundara Baalaji, K Ravi Acharya, T P Singh, S Krishnaswamy. 2005-07-30. High-resolution diffraction from crystals of a membrane-protein complex: bacterial outer membrane protein OmpC complexed with the antibacterial eukaryotic protein lactoferrin.. https://doi.org/10.1107/s1744309105022086

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