3LAA

Crystal structure of the trimeric autotransporter adhesin head domain BpaA from Burkholderia pseudomallei

Summary for 3LAA

• Entry DOI: 10.2210/pdb3laa/pdb
• Related: 3LA9
• Descriptor: Haemagglutinin family protein (2 entities in total)
• Functional Keywords: niaid, seattle structural genomics center for infectious disease, ssgcid, melioidosis, trimeric autotransporter, transport protein
• Biological source: Burkholderia pseudomallei
• Total number of polymer chains: 1
• Total formula weight: 19368.80

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2010-01-06, release date: 2010-05-12, Last modification date: 2023-09-06)

Primary citation

Edwards, T.E.,Phan, I.,Abendroth, J.,Dieterich, S.H.,Masoudi, A.,Guo, W.,Hewitt, S.N.,Kelley, A.,Leibly, D.,Brittnacher, M.J.,Staker, B.L.,Miller, S.I.,Van Voorhis, W.C.,Myler, P.J.,Stewart, L.J.
Structure of a Burkholderia pseudomallei trimeric autotransporter adhesin head.
Plos One, 5:12803-12811, 2010

PubMed Abstract: Pathogenic bacteria adhere to the host cell surface using a family of outer membrane proteins called Trimeric Autotransporter Adhesins (TAAs). Although TAAs are highly divergent in sequence and domain structure, they are all conceptually comprised of a C-terminal membrane anchoring domain and an N-terminal passenger domain. Passenger domains consist of a secretion sequence, a head region that facilitates binding to the host cell surface, and a stalk region.

PubMed: 20862217
DOI: 10.1371/journal.pone.0012803

Experimental method

X-RAY DIFFRACTION (1.35 Å)