Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC

F Cuskin; AS Solovyova; RJ Lewis; PR Race

doi:10.1107/s1744309111003484

Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC

F Cuskin, AS Solovyova, RJ Lewis, PR Race

School of Biochemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

6 Citations (Scopus)

Abstract

The antibiotic bacillaene is biosynthesized in Bacillus subtilis by a hybrid type 1 modular polyketide synthase/nonribosomal peptide synthetase of the transacyltransferase (trans-AT) class. Within this system, the essential acyl-group loading activity is provided by the action of three free-standing trans-acting acyltransferases. Here, the recombinant expression, purification and crystallization of the bacillaene synthase trans-acting acyltransferase PksC are reported. A diffraction data set has been collected from a single PksC crystal to 1.44 A ° resolution and the crystal was found to belong to the orthorhombic space group P212121.

Translated title of the contribution	Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC
Original language	English
Pages (from-to)	464 - 466
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	67
Issue number	4
DOIs	https://doi.org/10.1107/s1744309111003484
Publication status	Published - Apr 2011

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Structure and mechanism of a trans-acytransferase polyketide synthase
Race, P. R. (Principal Investigator)
19/09/11 → 19/09/14
Project: Research

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title = "Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC",

abstract = "The antibiotic bacillaene is biosynthesized in Bacillus subtilis by a hybrid type 1 modular polyketide synthase/nonribosomal peptide synthetase of the transacyltransferase (trans-AT) class. Within this system, the essential acyl-group loading activity is provided by the action of three free-standing trans-acting acyltransferases. Here, the recombinant expression, purification and crystallization of the bacillaene synthase trans-acting acyltransferase PksC are reported. A diffraction data set has been collected from a single PksC crystal to 1.44 A ° resolution and the crystal was found to belong to the orthorhombic space group P212121.",

author = "F Cuskin and AS Solovyova and RJ Lewis and PR Race",

year = "2011",

month = apr,

doi = "10.1107/s1744309111003484",

language = "English",

volume = "67",

pages = "464 -- 466",

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

issn = "1744-3091",

publisher = "Munksgaard International Publishers",

number = "4",

}

Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC. / Cuskin, F; Solovyova, AS; Lewis, RJ et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 4, 04.2011, p. 464 - 466.

Research output: Contribution to journal › Article (Academic Journal) › peer-review

TY - JOUR

T1 - Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC

AU - Cuskin, F

AU - Solovyova, AS

AU - Lewis, RJ

AU - Race, PR

PY - 2011/4

Y1 - 2011/4

N2 - The antibiotic bacillaene is biosynthesized in Bacillus subtilis by a hybrid type 1 modular polyketide synthase/nonribosomal peptide synthetase of the transacyltransferase (trans-AT) class. Within this system, the essential acyl-group loading activity is provided by the action of three free-standing trans-acting acyltransferases. Here, the recombinant expression, purification and crystallization of the bacillaene synthase trans-acting acyltransferase PksC are reported. A diffraction data set has been collected from a single PksC crystal to 1.44 A ° resolution and the crystal was found to belong to the orthorhombic space group P212121.

AB - The antibiotic bacillaene is biosynthesized in Bacillus subtilis by a hybrid type 1 modular polyketide synthase/nonribosomal peptide synthetase of the transacyltransferase (trans-AT) class. Within this system, the essential acyl-group loading activity is provided by the action of three free-standing trans-acting acyltransferases. Here, the recombinant expression, purification and crystallization of the bacillaene synthase trans-acting acyltransferase PksC are reported. A diffraction data set has been collected from a single PksC crystal to 1.44 A ° resolution and the crystal was found to belong to the orthorhombic space group P212121.

U2 - 10.1107/s1744309111003484

DO - 10.1107/s1744309111003484

M3 - Article (Academic Journal)

SN - 1744-3091

VL - 67

SP - 464

EP - 466

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 4

ER -

Crystallization and preliminary X-ray analysis of the bacillaene synthase trans-acting acyltransferase PksC

Abstract

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Structure and mechanism of a trans-acytransferase polyketide synthase

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