PDBsum entry 2a1c

Hormone/growth factor

PDB id

2a1c

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Contents

			Protein chain

					17 a.a.

PDB id:

2a1c

Links
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Name:

Hormone/growth factor

Title:

Solution structure of csp1

Structure:

Csp1. Chain: a. Synonym: competence stimulating peptide type 1. Engineered: yes

Source:

Synthetic: yes. Other_details: the peptide was chemically synthesized. This sequence occures naturally.

NMR struc:

20 models

Authors:

O.Johnsborg,P.E.Kristiansen

Key ref:

O.Johnsborg et al. (2006). A hydrophobic patch in the competence-stimulating Peptide, a pneumococcal competence pheromone, is essential for specificity and biological activity. J Bacteriol, 188, 1744-1749. PubMed id: 16484185

Date:

20-Jun-05

Release date:

30-May-06

PROCHECK

	Headers

	References

Protein chain

P60243 (CSP1_STRR6) - Competence-stimulating peptide type 1 from Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

Seq: Struc:					41 a.a. 17 a.a.

Key:

Secondary structure



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

	J Bacteriol 188:1744-1749 (2006)
PubMed id: 16484185

A hydrophobic patch in the competence-stimulating Peptide, a pneumococcal competence pheromone, is essential for specificity and biological activity.
O.Johnsborg, P.E.Kristiansen, T.Blomqvist, L.S.Håvarstein.

ABSTRACT

Induction of competence for natural genetic transformation in Streptococcus pneumoniae depends on pheromone-mediated cell-cell communication and a signaling pathway consisting of the competence-stimulating peptide (CSP), its membrane-embedded histidine kinase receptor ComD, and the cognate response regulator ComE. Extensive screening of pneumococcal isolates has revealed that two major CSP variants, CSP1 and CSP2, are found in members of this species. Even though the primary structures of CSP1 and CSP2 are about 50% identical, they are highly specific for their respective receptors, ComD1 and ComD2. In the present work, we have investigated the structural basis of this specificity by determining the three-dimensional structure of CSP1 from nuclear magnetic resonance data and comparing the agonist activity of a number of CSP1/CSP2 hybrid peptides toward the ComD1 and ComD2 receptors. Our results show that upon exposure to membrane-mimicking environments, the 17-amino-acid CSP1 pheromone adopts an amphiphilic alpha-helical configuration stretching from residue 6 to residue 12. Furthermore, the pattern of agonist activity displayed by the various hybrid peptides revealed that hydrophobic amino acids, some of which are situated on the nonpolar side of the alpha-helix, strongly contribute to CSP specificity. Together, these data indicate that the identified alpha-helix is an important structural feature of CSP1 which is essential for effective receptor recognition under natural conditions.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20543141

R.S.Harrison, N.E.Shepherd, H.N.Hoang, G.Ruiz-Gómez, T.A.Hill, R.W.Driver, V.S.Desai, P.R.Young, G.Abbenante, and D.P.Fairlie (2010).
Downsizing human, bacterial, and viral proteins to short water-stable alpha helices that maintain biological potency.

Proc Natl Acad Sci U S A, 107, 11686-11691.

20212168

W.L.Ng, Y.Wei, L.J.Perez, J.Cong, T.Long, M.Koch, M.F.Semmelhack, N.S.Wingreen, and B.L.Bassler (2010).
Probing bacterial transmembrane histidine kinase receptor-ligand interactions with natural and synthetic molecules.

Proc Natl Acad Sci U S A, 107, 5575-5580.

19517207

X.Tian, R.T.Syvitski, T.Liu, N.Livingstone, D.L.Jakeman, and Y.H.Li (2009).
A method for structure-activity analysis of quorum-sensing signaling peptides from naturally transformable streptococci.

Biol Proced Online, 11, 207-226.

17229063

E.Allan, H.A.Hussain, K.R.Crawford, S.Miah, Z.K.Ascott, M.H.Khwaja, and A.H.Hosie (2007).
Genetic variation in comC, the gene encoding competence-stimulating peptide (CSP) in Streptococcus mutans.

FEMS Microbiol Lett, 268, 47-51.

17098891

K.R.Fixen, J.R.Chandler, T.Le, B.K.Kozlowicz, D.A.Manias, and G.M.Dunny (2007).
Analysis of the amino acid sequence specificity determinants of the enterococcal cCF10 sex pheromone in interactions with the pheromone-sensing machinery.

J Bacteriol, 189, 1399-1406.

16936029

R.T.Syvitski, X.L.Tian, K.Sampara, A.Salman, S.F.Lee, D.L.Jakeman, and Y.H.Li (2007).
Structure-activity analysis of quorum-sensing signaling peptides from Streptococcus mutans.

J Bacteriol, 189, 1441-1450.

PDB codes:

2i2h 2i2j

16925560

F.C.Petersen, G.Fimland, and A.A.Scheie (2006).
Purification and functional studies of a potent modified quorum-sensing peptide and a two-peptide bacteriocin in Streptococcus mutans.

Mol Microbiol, 61, 1322-1334.

16923913

H.Ichihara, K.Kuma, and H.Toh (2006).
Positive selection in the ComC-ComD system of Streptococcal Species.

J Bacteriol, 188, 6429-6434.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.