Ontology highlight
ABSTRACT:
SUBMITTER: Xu Q
PROVIDER: S-EPMC2954219 | biostudies-literature | 2010 Oct
REPOSITORIES: biostudies-literature
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]