The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster

Greg Mann; Jesko Koehnke; Andrew F. Bent; Rachael Graham; Wael Houssen; Marcel Jaspars; Uli Schwarz-Linek; James H. Naismith

doi:10.1107/S2053230X1402425X

The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster

Greg Mann
, Jesko Koehnke
, Andrew F. Bent
, Rachael Graham
, Wael Houssen
, Marcel Jaspars
, Uli Schwarz-Linek
, James H. Naismith^*

^*Corresponding author for this work

University of St Andrews
Mansoura University

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

16 Citations (Scopus)

15 Downloads (Pure)

Abstract

Patellamides are members of the cyanobactin family of ribosomally synthesized and post-translationally modified cyclic peptide natural products, many of which, including some patellamides, are biologically active. A detailed mechanistic understanding of the biosynthetic pathway would enable the construction of a biotechnological 'toolkit' to make novel analogues of patellamides that are not found in nature. All but two of the protein domains involved in patellamide biosynthesis have been characterized. The two domains of unknown function (DUFs) are homologous to each other and are found at the C-termini of the multi-domain proteins PatA and PatG. The domain sequence is found in all cyanobactin-biosynthetic pathways characterized to date, implying a functional role in cyanobactin biosynthesis. Here, the crystal structure of the PatG DUF domain is reported and its binding interactions with plausible substrates are investigated.

Original language	English
Pages (from-to)	1597-1603
Number of pages	7
Journal	Acta Crystallographica Section F: Structural Biology Communications
Volume	70
Issue number	12
Early online date	Nov 2014
DOIs	https://doi.org/10.1107/S2053230X1402425X
Publication status	Published - Dec 2014

Funding

We thank the staff of beamline I02 at the Diamond Light Source for their support with data collection. Thanks go to the NMR and BSRC mass-spectrometry facilities at the University of St Andrews for crucial support. This work was funded by the BBSRC (BB/K015508/1) and ERC (TNT-LEAP), and the University of St Andrews infrastructure is supported by a Wellcome Trust Capital Award (086036). WH is the recipient of the SULSA Leaders award.

Keywords

LISSOCLINUM-PATELLA
PROCHLORON-DIDEMNI
PROTEIN-STRUCTURE
ALIGNMENT
PATHWAY
SINGLE
SYSTEM

Access to Document

10.1107/S2053230X1402425XLicence: CC BY

The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster
This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. http://creativecommons.org/licenses/by/4.0/
Final published version, 1.49 MBLicence: CC BY

Cite this

@article{f27f689115484763925d8c259209c2d9,

title = "The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster",

abstract = "Patellamides are members of the cyanobactin family of ribosomally synthesized and post-translationally modified cyclic peptide natural products, many of which, including some patellamides, are biologically active. A detailed mechanistic understanding of the biosynthetic pathway would enable the construction of a biotechnological 'toolkit' to make novel analogues of patellamides that are not found in nature. All but two of the protein domains involved in patellamide biosynthesis have been characterized. The two domains of unknown function (DUFs) are homologous to each other and are found at the C-termini of the multi-domain proteins PatA and PatG. The domain sequence is found in all cyanobactin-biosynthetic pathways characterized to date, implying a functional role in cyanobactin biosynthesis. Here, the crystal structure of the PatG DUF domain is reported and its binding interactions with plausible substrates are investigated.",

keywords = "LISSOCLINUM-PATELLA, PROCHLORON-DIDEMNI, PROTEIN-STRUCTURE, ALIGNMENT, PATHWAY, SINGLE, SYSTEM",

author = "Greg Mann and Jesko Koehnke and Bent, \{Andrew F.\} and Rachael Graham and Wael Houssen and Marcel Jaspars and Uli Schwarz-Linek and Naismith, \{James H.\}",

year = "2014",

month = dec,

doi = "10.1107/S2053230X1402425X",

language = "English",

volume = "70",

pages = "1597--1603",

journal = "Acta Crystallographica Section F: Structural Biology Communications ",

issn = "2053-230X",

publisher = "International Union of Crystallography",

number = "12",

}

TY - JOUR

T1 - The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster

AU - Mann, Greg

AU - Koehnke, Jesko

AU - Bent, Andrew F.

AU - Graham, Rachael

AU - Houssen, Wael

AU - Jaspars, Marcel

AU - Schwarz-Linek, Uli

AU - Naismith, James H.

PY - 2014/12

Y1 - 2014/12

N2 - Patellamides are members of the cyanobactin family of ribosomally synthesized and post-translationally modified cyclic peptide natural products, many of which, including some patellamides, are biologically active. A detailed mechanistic understanding of the biosynthetic pathway would enable the construction of a biotechnological 'toolkit' to make novel analogues of patellamides that are not found in nature. All but two of the protein domains involved in patellamide biosynthesis have been characterized. The two domains of unknown function (DUFs) are homologous to each other and are found at the C-termini of the multi-domain proteins PatA and PatG. The domain sequence is found in all cyanobactin-biosynthetic pathways characterized to date, implying a functional role in cyanobactin biosynthesis. Here, the crystal structure of the PatG DUF domain is reported and its binding interactions with plausible substrates are investigated.

AB - Patellamides are members of the cyanobactin family of ribosomally synthesized and post-translationally modified cyclic peptide natural products, many of which, including some patellamides, are biologically active. A detailed mechanistic understanding of the biosynthetic pathway would enable the construction of a biotechnological 'toolkit' to make novel analogues of patellamides that are not found in nature. All but two of the protein domains involved in patellamide biosynthesis have been characterized. The two domains of unknown function (DUFs) are homologous to each other and are found at the C-termini of the multi-domain proteins PatA and PatG. The domain sequence is found in all cyanobactin-biosynthetic pathways characterized to date, implying a functional role in cyanobactin biosynthesis. Here, the crystal structure of the PatG DUF domain is reported and its binding interactions with plausible substrates are investigated.

KW - LISSOCLINUM-PATELLA

KW - PROCHLORON-DIDEMNI

KW - PROTEIN-STRUCTURE

KW - ALIGNMENT

KW - PATHWAY

KW - SINGLE

KW - SYSTEM

U2 - 10.1107/S2053230X1402425X

DO - 10.1107/S2053230X1402425X

M3 - Article

SN - 2053-230X

VL - 70

SP - 1597

EP - 1603

JO - Acta Crystallographica Section F: Structural Biology Communications

JF - Acta Crystallographica Section F: Structural Biology Communications

IS - 12

ER -

The structure of the cyanobactin domain of unknown function from PatG in the patellamide gene cluster

Abstract

Funding

Keywords

Access to Document

Fingerprint

Cite this