TY - JOUR
T1 - The structure of pyogenecin immunity protein, a novel bacteriocin-like immunity protein from Streptococcus pyogenes
AU - Chang, Changsoo
AU - Coggill, Penny
AU - Bateman, Alex
AU - Finn, Robert D.
AU - Cymborowski, Marcin
AU - Otwinowski, Zbyszek
AU - Minor, Wladek
AU - Volkart, Lour
AU - Joachimiak, Andrzej
N1 - Funding Information:
The authors wish to thank members of The Structural Biology Center at Argonne National Laboratory for their help with data collection at the 19ID beamline. We also thank Lindsey Butler for help in preparation of this manuscript. This work was supported by National Institutes of Health grant GM074942 and by the U. S. Department of Energy, Office of Biological and Environmental Research, under contract DE-AC02-06CH11357. PC, AB and RDF are funded by the Wellcome Trust and this work was supported by the Wellcome Trust [grant number WT077044/Z/05/Z]. The submitted manuscript has been created by UChicago Argonne, LLC, Operator of Argonne National Laboratory ("Argonne"). Argonne, a U.S. Department of Energy Office of Science laboratory, is operated under Contract No. DE-AC02-06CH11357. The U.S. Government retains for itself, and others acting on its behalf, a paid-up nonexclusive, irrevocable worldwide license in said article to reproduce, prepare derivative works, distribute copies to the public, and perform publicly and display publicly, by or on behalf of the Government.
PY - 2009
Y1 - 2009
N2 - Background. Many Gram-positive lactic acid bacteria (LAB) produce anti-bacterial peptides and small proteins called bacteriocins, which enable them to compete against other bacteria in the environment. These peptides fall structurally into three different classes, I, II, III, with class IIa being pediocin-like single entities and class IIb being two-peptide bacteriocins. Self-protective cognate immunity proteins are usually co-transcribed with these toxins. Several examples of cognates for IIa have already been solved structurally. Streptococcus pyogenes, closely related to LAB, is one of the most common human pathogens, so knowledge of how it competes against other LAB species is likely to prove invaluable. Results. We have solved the crystal structure of the gene-product of locus Spy-2152 from S. pyogenes, (PDB:2fu2), and found it to comprise an anti-parallel four-helix bundle that is structurally similar to other bacteriocin immunity proteins. Sequence analyses indicate this protein to be a possible immunity protein protective against class IIa or IIb bacteriocins. However, given that S. pyogenes appears to lack any IIa pediocin-like proteins but does possess class IIb bacteriocins, we suggest this protein confers immunity to IIb-like peptides. Conclusions. Combined structural, genomic and proteomic analyses have allowed the identification and in silico characterization of a new putative immunity protein from S. pyogenes, possibly the first structure of an immunity protein protective against potential class IIb two-peptide bacteriocins. We have named the two pairs of putative bacteriocins found in S. pyogenes pyogenecin 1, 2, 3 and 4.
AB - Background. Many Gram-positive lactic acid bacteria (LAB) produce anti-bacterial peptides and small proteins called bacteriocins, which enable them to compete against other bacteria in the environment. These peptides fall structurally into three different classes, I, II, III, with class IIa being pediocin-like single entities and class IIb being two-peptide bacteriocins. Self-protective cognate immunity proteins are usually co-transcribed with these toxins. Several examples of cognates for IIa have already been solved structurally. Streptococcus pyogenes, closely related to LAB, is one of the most common human pathogens, so knowledge of how it competes against other LAB species is likely to prove invaluable. Results. We have solved the crystal structure of the gene-product of locus Spy-2152 from S. pyogenes, (PDB:2fu2), and found it to comprise an anti-parallel four-helix bundle that is structurally similar to other bacteriocin immunity proteins. Sequence analyses indicate this protein to be a possible immunity protein protective against class IIa or IIb bacteriocins. However, given that S. pyogenes appears to lack any IIa pediocin-like proteins but does possess class IIb bacteriocins, we suggest this protein confers immunity to IIb-like peptides. Conclusions. Combined structural, genomic and proteomic analyses have allowed the identification and in silico characterization of a new putative immunity protein from S. pyogenes, possibly the first structure of an immunity protein protective against potential class IIb two-peptide bacteriocins. We have named the two pairs of putative bacteriocins found in S. pyogenes pyogenecin 1, 2, 3 and 4.
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U2 - 10.1186/1472-6807-9-75
DO - 10.1186/1472-6807-9-75
M3 - Article
C2 - 20017931
AN - SCOPUS:74349107323
SN - 1472-6807
VL - 9
JO - BMC Structural Biology
JF - BMC Structural Biology
M1 - 75
ER -