Document Detail


Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicron.
MedLine Citation:
PMID:  20944225     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Qingping Xu; Polat Abdubek; Tamara Astakhova; Herbert L Axelrod; Constantina Bakolitsa; Xiaohui Cai; Dennis Carlton; Connie Chen; Hsiu Ju Chiu; Thomas Clayton; Debanu Das; Marc C Deller; Lian Duan; Kyle Ellrott; Carol L Farr; Julie Feuerhelm; Joanna C Grant; Anna Grzechnik; Gye Won Han; Lukasz Jaroszewski; Kevin K Jin; Heath E Klock; Mark W Knuth; Piotr Kozbial; S Sri Krishna; Abhinav Kumar; Winnie W Lam; David Marciano; Mitchell D Miller; Andrew T Morse; Edward Nigoghossian; Amanda Nopakun; Linda Okach; Christina Puckett; Ron Reyes; Henry J Tien; Christine B Trame; Henry van den Bedem; Dana Weekes; Tiffany Wooten; Andrew Yeh; Jiadong Zhou; Keith O Hodgson; John Wooley; Marc André Elsliger; Ashley M Deacon; Adam Godzik; Scott A Lesley; Ian A Wilson
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2010-07-31
Journal Detail:
Title:  Acta crystallographica. Section F, Structural biology and crystallization communications     Volume:  66     ISSN:  1744-3091     ISO Abbreviation:  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-10-14     Completed Date:  2011-01-28     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  101226117     Medline TA:  Acta Crystallogr Sect F Struct Biol Cryst Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  1297-305     Citation Subset:  IM    
Affiliation:
Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
Data Bank Information
Bank Name/Acc. No.:
PDB/3KK7
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry*
Bacteroides / chemistry*
Crystallography, X-Ray
Models, Molecular
Molecular Sequence Data
Perforin / chemistry*
Protein Structure, Tertiary
Sequence Alignment
Structural Homology, Protein
Grant Support
ID/Acronym/Agency:
U54 GM074898/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 126465-35-8/Perforin
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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