Browse views: by Year, by Function, by GLF, by Subfunction, by Conference, by Journal

GNF ID 100604: Crystal structure of a membrane attack complex/perforin (MACPF) family protein from a human gut symbiont Bacteroides thetaiotaomicron

Xu, Qingping and Abdubeck, Polat and Chen, Connie and Feuerhelm, Julie and Grant, Joanna and Klock, Heath and Knuth, Mark and Nigoghossian, Edward and Okach, Linda and Puckett, Christina and Wooten, Tiffany and Zhou, Jiadong and Lesley, Scott and Stolz, Barbara (2010) GNF ID 100604: Crystal structure of a membrane attack complex/perforin (MACPF) family protein from a human gut symbiont Bacteroides thetaiotaomicron. Acta F.

Abstract

Membrane attack complex/perforin (MACPF) proteins are transmembrane pore-forming
proteins that are important in both human immunity and virulence of pathogens. Bacterial MACPFs
are found in diverse bacterial species, including most human gut-associated Bacteroides. We
determined the crystal structure of a bacterial MACPF domain containing protein BT_3439 (Bth-
MACPF) from Bacteroides thetaiotaomicron, a predominant member of mammalian intestinal
microbiota. Bth-MACPF contains a membrane attack complex/perforin (MACPF) domain, and two
novel C-terminal domains that resemble ribonuclease H and interleukin 8 respectively. However, the
entire protein adopts a flat, crescent shape characteristic of MACPF proteins, which may be
important for oligomerization. This Bth-MACPF structure supplements knowledge of MACPF
proteins obtained previously from two other MACPF structures. Genomic context analysis infers
that Bth-MACPF may be involved in a novel protein transport or nutrient uptake system, suggesting
the potential importance of these MACPF proteins of eukaryotic origin in the adaption of
commensal bacteria to the host environment.

Item Type: Article
Additional Information: grant requirement B. Stolz is NOT an author -- NVS contact person for GNF manuscript approval. This manuscript shall NOT be copied to the OAK internet.
Keywords: MACPF, Membrane attack complex, Perforin, transmembrane pores, pathogenesis
Date Deposited: 13 Oct 2015 13:16
Last Modified: 13 Oct 2015 13:16
URI: https://oak.novartis.com/id/eprint/3111

Search

Email Alerts

Register with OAK to receive email alerts for saved searches.