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Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicron.


ABSTRACT: Membrane-attack complex/perforin (MACPF) proteins are transmembrane pore-forming proteins that are important in both human immunity and the virulence of pathogens. Bacterial MACPFs are found in diverse bacterial species, including most human gut-associated Bacteroides species. The crystal structure of a bacterial MACPF-domain-containing protein BT_3439 (Bth-MACPF) from B. thetaiotaomicron, a predominant member of the mammalian intestinal microbiota, has been determined. Bth-MACPF contains a membrane-attack complex/perforin (MACPF) domain and two novel C-terminal domains that resemble ribonuclease H and interleukin 8, respectively. The entire protein adopts a flat crescent shape, characteristic of other MACPF proteins, that may be important for oligomerization. This Bth-MACPF structure provides new features and insights not observed in two previous MACPF structures. Genomic context analysis infers that Bth-MACPF may be involved in a novel protein-transport or nutrient-uptake system, suggesting an important role for these MACPF proteins, which were likely to have been inherited from eukaryotes via horizontal gene transfer, in the adaptation of commensal bacteria to the host environment.

SUBMITTER: Xu Q 

PROVIDER: S-EPMC2954219 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

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Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicron.

Xu Qingping Q   Abdubek Polat P   Astakhova Tamara T   Axelrod Herbert L HL   Bakolitsa Constantina C   Cai Xiaohui X   Carlton Dennis D   Chen Connie C   Chiu Hsiu Ju HJ   Clayton Thomas T   Das Debanu D   Deller Marc C MC   Duan Lian L   Ellrott Kyle K   Farr Carol L CL   Feuerhelm Julie J   Grant Joanna C JC   Grzechnik Anna A   Han Gye Won GW   Jaroszewski Lukasz L   Jin Kevin K KK   Klock Heath E HE   Knuth Mark W MW   Kozbial Piotr P   Krishna S Sri SS   Kumar Abhinav A   Lam Winnie W WW   Marciano David D   Miller Mitchell D MD   Morse Andrew T AT   Nigoghossian Edward E   Nopakun Amanda A   Okach Linda L   Puckett Christina C   Reyes Ron R   Tien Henry J HJ   Trame Christine B CB   van den Bedem Henry H   Weekes Dana D   Wooten Tiffany T   Yeh Andrew A   Zhou Jiadong J   Hodgson Keith O KO   Wooley John J   Elsliger Marc André MA   Deacon Ashley M AM   Godzik Adam A   Lesley Scott A SA   Wilson Ian A IA  

Acta crystallographica. Section F, Structural biology and crystallization communications 20100731 Pt 10


Membrane-attack complex/perforin (MACPF) proteins are transmembrane pore-forming proteins that are important in both human immunity and the virulence of pathogens. Bacterial MACPFs are found in diverse bacterial species, including most human gut-associated Bacteroides species. The crystal structure of a bacterial MACPF-domain-containing protein BT_3439 (Bth-MACPF) from B. thetaiotaomicron, a predominant member of the mammalian intestinal microbiota, has been determined. Bth-MACPF contains a memb  ...[more]

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