Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3D9X

Structure of the head of the Bartonella adhesin BadA

Summary for 3D9X
Entry DOI10.2210/pdb3d9x/pdb
DescriptorAdhesin A (2 entities in total)
Functional Keywordsbada, trimeric adhesin, structure modules, high resolution, cell adhesion
Biological sourceBartonella henselae
Total number of polymer chains3
Total formula weight51594.55
Authors
Zeth, K.,Lupas, A.,Martin, J. (deposition date: 2008-05-28, release date: 2008-08-26, Last modification date: 2023-11-01)
Primary citationSzczesny, P.,Linke, D.,Ursinus, A.,Bar, K.,Schwarz, H.,Riess, T.M.,Kempf, V.A.,Lupas, A.N.,Martin, J.,Zeth, K.
Structure of the head of the Bartonella adhesin BadA
Plos Pathog., 4:e1000119-e1000119, 2008
Cited by
PubMed 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 domains were not recognizably similar to any protein of known structure. We therefore determined their crystal structure to a resolution of 1.1 A. Both domains are beta-prisms, the N-terminal one formed by interleaved, five-stranded beta-meanders parallel to the trimer axis and the C-terminal one by five-stranded beta-meanders orthogonal to the axis. Despite the absence of statistically significant sequence similarity, the two domains are structurally similar to domains from Haemophilus Hia, albeit in permuted order. Thus, the BadA head appears to be a chimera of domains seen in two other TAAs, YadA and Hia, highlighting the combinatorial evolutionary strategy taken by pathogens.
PubMed: 18688279
DOI: 10.1371/journal.ppat.1000119
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.13 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon