Structure of the Bartonella Adhesin BadA
Author Information
Author(s): Szczesny Pawel, Linke Dirk, Ursinus Astrid, Bär Kerstin, Schwarz Heinz, Riess Tanja M., Kempf Volkhard A. J., Lupas Andrei N., Martin Jörg, Zeth Kornelius
Primary Institution: Max Planck Institute for Developmental Biology, Tübingen, Germany
Hypothesis
The study aims to determine the crystal structure of the head of the Bartonella adhesin BadA.
Conclusion
The structure of the BadA head reveals a novel assembly of domains that are structurally similar to those found in other trimeric autotransporter adhesins.
Supporting Evidence
- The BadA head consists of two domains that are structurally similar to domains from Haemophilus Hia.
- The study highlights a combinatorial evolutionary strategy taken by pathogens in developing adhesive proteins.
- The crystal structure was determined to a resolution of 1.1 Å.
Takeaway
Scientists figured out how a protein that helps bacteria stick to surfaces is built, showing it uses parts from other similar proteins in a new way.
Methodology
The researchers used X-ray crystallography to determine the structure of the BadA head domains.
Limitations
The study does not address the functional implications of the structural findings in vivo.
Digital Object Identifier (DOI)
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