6XI1

Crystal structure of tetra-tandem repeat in extending RTX adhesin from Aeromonas hydrophila

This is a non-PDB format compatible entry.

Summary for 6XI1

• Entry DOI: 10.2210/pdb6xi1/pdb
• Descriptor: Flagellin hook IN motif family, GLYCEROL, CHLORIDE ION, ... (7 entities in total)
• Functional Keywords: beta-sandwich domains, bacterial adhesin, rtx protein, adhesion protein, calcium binding protein, vcbs-repeat, metal binding protein
• Biological source: Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
• Total number of polymer chains: 2
• Total formula weight: 93009.27

Authors

Ye, Q.,Vance, T.D.R.,Conroy, B.,Davies, P.L. (deposition date: 2020-06-19, release date: 2020-10-14, Last modification date: 2024-03-06)

Primary citation

Vance, T.D.R.,Ye, Q.,Conroy, B.,Davies, P.L.
Essential role of calcium in extending RTX adhesins to their target.
J Struct Biol X, 4:100036-100036, 2020

PubMed Abstract: RTX adhesins are long, multi-domain proteins present on the outer membrane of many Gram-negative bacteria. From this vantage point, adhesins use their distal ligand-binding domains for surface attachment leading to biofilm formation. To expand the reach of the ligand-binding domains, RTX adhesins maintain a central extender region of multiple tandem repeats, which makes up most of the proteins' large molecular weight. Alignments of the 10-15-kDa extender domains show low sequence identity between adhesins. Here we have produced and structurally characterized protein constructs of four tandem repeats (tetra-tandemers) from two different RTX adhesins. In comparing the tetra-tandemers to each other and already solved structures from and , the extender domains fold as diverse beta-sandwich structures with widely differing calcium contents. However, all the tetra-tandemers have at least one calcium ion coordinated in the linker region between beta-sandwich domains whose role appears to be the rigidification of the extender region to help the adhesin extend its reach.

PubMed: 32984811
DOI: 10.1016/j.yjsbx.2020.100036

Experimental method

X-RAY DIFFRACTION (1.75 Å)