3KK7
Crystal structure of Putative cell invasion protein with MAC/Perforin domain (NP_812351.1) from BACTERIODES THETAIOTAOMICRON VPI-5482 at 2.46 A resolution
Summary for 3KK7
Entry DOI | 10.2210/pdb3kk7/pdb |
Descriptor | Putative cell invasion protein with MAC/Perforin domain, CHLORIDE ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | putative cell invasion protein with mac/perforin domain, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, cell invasion |
Biological source | Bacteroides thetaiotaomicron VPI-5482 |
Total number of polymer chains | 2 |
Total formula weight | 124354.59 |
Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2009-11-04, release date: 2009-11-24, Last modification date: 2024-11-06) |
Primary citation | Xu, Q.,Abdubek, P.,Astakhova, T.,Axelrod, H.L.,Bakolitsa, C.,Cai, X.,Carlton, D.,Chen, C.,Chiu, H.J.,Clayton, T.,Das, D.,Deller, M.C.,Duan, L.,Ellrott, K.,Farr, C.L.,Feuerhelm, J.,Grant, J.C.,Grzechnik, A.,Han, G.W.,Jaroszewski, L.,Jin, K.K.,Klock, H.E.,Knuth, M.W.,Kozbial, P.,Krishna, S.S.,Kumar, A.,Lam, W.W.,Marciano, D.,Miller, M.D.,Morse, A.T.,Nigoghossian, E.,Nopakun, A.,Okach, L.,Puckett, C.,Reyes, R.,Tien, H.J.,Trame, C.B.,van den Bedem, H.,Weekes, D.,Wooten, T.,Yeh, A.,Zhou, J.,Hodgson, K.O.,Wooley, J.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Wilson, I.A. Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicron. Acta Crystallogr.,Sect.F, 66:1297-1305, 2010 Cited by PubMed 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. PubMed: 20944225DOI: 10.1107/S1744309110023055 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.46 Å) |
Structure validation
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