structure of the head of the bartonella adhesin bada结构的巴尔通氏体属adhesin巴达.pdfVIP

Structure of the Head of the Bartonella Adhesin BadA 1,2 1 1 ¨ 1 1 3 Pawel Szczesny , Dirk Linke , Astrid Ursinus , Kerstin Bar , Heinz Schwarz , Tanja M. Riess , 3 1 ¨ 1 1 Volkhard A. J. Kempf , Andrei N. Lupas *, Jorg Martin , Kornelius Zeth ¨ 1 Department of Protein Evolution, Max Planck Institute for Developmental Biology, Tubingen, Germany, 2 Department of Bioinformatics, Institute of Biochemistry and ¨ ¨ ¨ Biophysics, Polish Academy of Sciences, Warsaw, Poland, 3 Institut fur Medizinische Mikrobiologie und Hygiene, Eberhard-Karls-Universitat, Tubingen, Germany Abstract Trimeric autotransporter adhesins (TAAs) are a major class of proteins by which pathogenic proteobacteria adhere to their hosts. Prominent examples include Yersinia YadA, Haemophilus Hia and Hsf, Moraxella UspA1 and A2, and Neisseria NadA. TAAs also occur in symbiotic and environmental species and presumably represent a general solution to the problem of adhesion in proteobacteria. The general structure of TAAs follows a head-stalk-anchor architecture, where the heads are the primary mediators of attachment and autoagglutination. In the major adhesin of Bartonella henselae, BadA, the head consists of three domains, the N-terminal of which shows strong sequence similarity to the head of Yersinia YadA. The two other do