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Crystal structure of 527-665 fragment of UspA1 protein from Moraxella catarrhalisCrystal structure of 527-665 fragment of UspA1 protein from Moraxella catarrhalis
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMoraxella catarrhalis is a ubiquitous human-specific bacterium commonly associated with upper and lower respiratory tract infections, including otitis media, sinusitis and chronic obstructive pulmonary disease. The bacterium uses an autotransporter protein UspA1 to target an important human cellular receptor carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1). Using X-ray crystallography, we show that the CEACAM1 receptor-binding region of UspA1 unusually consists of an extended, rod-like left-handed trimeric coiled-coil. Mutagenesis and binding studies of UspA1 and the N-domain of CEACAM1 have been used to delineate the interacting surfaces between ligand and receptor and guide assembly of the complex. However, solution scattering, molecular modelling and electron microscopy analyses all indicate that significant bending of the UspA1 coiled-coil stalk also occurs. This explains how UspA1 can engage CEACAM1 at a site far distant from its head group, permitting closer proximity of the respective cell surfaces during infection. The Moraxella adhesin UspA1 binds to its human CEACAM1 receptor by a deformable trimeric coiled-coil.,Conners R, Hill DJ, Borodina E, Agnew C, Daniell SJ, Burton NM, Sessions RB, Clarke AR, Catto LE, Lammie D, Wess T, Brady RL, Virji M EMBO J. 2008 Jun 18;27(12):1779-89. Epub 2008 May 22. PMID:18497748[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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