7AVH

Streptococcal High Identity Repeats in Tandem (SHIRT) domains 3-4 from cell surface protein SGO_0707

Summary for 7AVH

• Entry DOI: 10.2210/pdb7avh/pdb
• Related: 5LRH
• Descriptor: LPXTG cell wall surface protein, CHLORIDE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: bacterial surface, adhesin, tandem repeat, sgo0707, cell adhesion
• Biological source: Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
• Total number of polymer chains: 1
• Total formula weight: 18536.58

Authors

Whelan, F.,Jenkins, H.T.,Potts, J.R. (deposition date: 2020-11-05, release date: 2021-06-09, Last modification date: 2024-05-01)

Primary citation

Whelan, F.,Lafita, A.,Gilburt, J.,Degut, C.,Griffiths, S.C.,Jenkins, H.T.,St John, A.N.,Paci, E.,Moir, J.W.B.,Plevin, M.J.,Baumann, C.G.,Bateman, A.,Potts, J.R.
Periscope Proteins are variable-length regulators of bacterial cell surface interactions.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Changes at the cell surface enable bacteria to survive in dynamic environments, such as diverse niches of the human host. Here, we reveal "Periscope Proteins" as a widespread mechanism of bacterial surface alteration mediated through protein length variation. Tandem arrays of highly similar folded domains can form an elongated rod-like structure; thus, variation in the number of domains determines how far an N-terminal host ligand binding domain projects from the cell surface. Supported by newly available long-read genome sequencing data, we propose that this class could contain over 50 distinct proteins, including those implicated in host colonization and biofilm formation by human pathogens. In large multidomain proteins, sequence divergence between adjacent domains appears to reduce interdomain misfolding. Periscope Proteins break this "rule," suggesting that their length variability plays an important role in regulating bacterial interactions with host surfaces, other bacteria, and the immune system.

PubMed: 34074781
DOI: 10.1073/pnas.2101349118

Experimental method

X-RAY DIFFRACTION (1.35 Å)