Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1–34

Wael E Houssen; Stephen Henry Wright; Arnout P. Kalverda; Gary S. Thompson; Sharon M. Kelly; Marcel Jaspars

doi:10.1002/cbic.201000305

Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1–34

Wael E Houssen , Stephen Henry Wright, Arnout P. Kalverda, Gary S. Thompson, Sharon M. Kelly, Marcel Jaspars

University of Leeds

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an a-helix spanning residues 13-28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes.

Original language	English
Pages (from-to)	1867-1873
Number of pages	7
Journal	ChemBioChem
Volume	11
Issue number	13
Early online date	16 Aug 2010
DOIs	https://doi.org/10.1002/cbic.201000305
Publication status	Published - 3 Sept 2010

Keywords

biosynthesis
cyanobactins
patellamides
peptides
Prochloron
protein secondary structure
2-dimensional NMR-spectroscopy
carboxylation recognition site
microcin B17
mutational analysis
lissoclinum-patella
escherichia-coli
natural-product
gene-cluster

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10.1002/cbic.201000305

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title = "Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1–34",

abstract = "The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an a-helix spanning residues 13-28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes.",

keywords = "biosynthesis, cyanobactins, patellamides, peptides, Prochloron, protein secondary structure, 2-dimensional NMR-spectroscopy, carboxylation recognition site, microcin B17, mutational analysis, lissoclinum-patella, escherichia-coli, natural-product, gene-cluster",

author = "Houssen, {Wael E} and Wright, {Stephen Henry} and Kalverda, {Arnout P.} and Thompson, {Gary S.} and Kelly, {Sharon M.} and Marcel Jaspars",

year = "2010",

month = sep,

day = "3",

doi = "10.1002/cbic.201000305",

language = "English",

volume = "11",

pages = "1867--1873",

journal = "ChemBioChem",

issn = "1439-4227",

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TY - JOUR

T1 - Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1–34

AU - Houssen , Wael E

AU - Wright, Stephen Henry

AU - Kalverda, Arnout P.

AU - Thompson, Gary S.

AU - Kelly, Sharon M.

AU - Jaspars, Marcel

PY - 2010/9/3

Y1 - 2010/9/3

N2 - The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an a-helix spanning residues 13-28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes.

AB - The solution structure of the leader sequence of the patellamide precursor peptide was analysed by using CD and determined with NOE-restrained molecular dynamics calculations. This leader sequence is highly conserved in the precursor peptides of some other cyanobactins harbouring heterocycles, and is assumed to play a role in targeting the precursor peptide to the post-translational machinery. The sequence was observed to form an a-helix spanning residues 13-28 with a hydrophobic surface on one side of the helix. This hydrophobic surface is proposed to be the site of the initial binding with modifying enzymes.

KW - biosynthesis

KW - cyanobactins

KW - patellamides

KW - peptides

KW - Prochloron

KW - protein secondary structure

KW - 2-dimensional NMR-spectroscopy

KW - carboxylation recognition site

KW - microcin B17

KW - mutational analysis

KW - lissoclinum-patella

KW - escherichia-coli

KW - natural-product

KW - gene-cluster

U2 - 10.1002/cbic.201000305

DO - 10.1002/cbic.201000305

M3 - Article

SN - 1439-4227

VL - 11

SP - 1867

EP - 1873

JO - ChemBioChem

JF - ChemBioChem

IS - 13

ER -

Solution Structure of the Leader Sequence of the Patellamide Precursor Peptide, PatE1–34

Abstract

Keywords

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