title: Expression, purification, crystallization and preliminary X-ray analysis of the extracellular sensory domain of DraK histidine kinase from Streptomyces coelicolor.
abstract: The bacterium Streptomyces coelicolor produces useful antibiotics from its secondary metabolites. DraK is a sensory histidine kinase involved in the differential regulation of antibiotics in S. coelicolor through the DraR/DraK two-component system. Here, the extracellular sensory domain of DraK was overexpressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method. The crystal diffracted to 2.2 Å resolution and belonged to space group C222₁, with unit-cell parameters a = 41.91, b = 174.50, c = 145.25 Å, α = β = γ = 90°.
authors.affiliation: Division of Magnetic Resonance, Korea Basic Science Institute, 16 Yeongudanji-Ro, Ochang, Chungbuk 363-883, Republic of Korea.
authors.forename: Kwon Joo
authors.initials: KJ
authors.lastname: Yeo
authors.forename: Young-Hyun
authors.initials: YH
authors.lastname: Han
authors.forename: Yumi
authors.initials: Y
authors.lastname: Eo
authors.forename: Hae-Kap
authors.initials: HK
authors.lastname: Cheong
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D045604:Extracellular Fluid / Q000201:enzymology*; D015964:Gene Expression Regulation, Bacterial; D000071677:Histidine Kinase; D011494:Protein Kinases / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D048372:Streptomyces coelicolor / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D011494:Protein Kinases; D000071677:Histidine Kinase
keywords: DraK; SCO3062; Streptomyces coelicolor; histidine kinases; two-component systems
references.citation: Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):458-64
references.pmid: 15805601
references.citation: J Biol Chem. 2003 Oct 3;278(40):39185-8
references.pmid: 12907689
references.citation: Biochem Biophys Res Commun. 2013 Feb 15;431(3):554-9
references.pmid: 23321311
references.citation: Science. 1989 Feb 24;243(4894 Pt 1):1059-62
references.pmid: 2646710
references.citation: Methods Enzymol. 1997;276:307-26
references.pmid: 27754618
references.citation: Curr Opin Struct Biol. 2010 Dec;20(6):763-71
references.pmid: 20951027
references.citation: J Mol Biol. 2008 Mar 21;377(2):512-23
references.pmid: 18258261
references.citation: Proc Natl Acad Sci U S A. 2003 Nov 25;100 Suppl 2:14555-61
references.pmid: 12970466
references.citation: J Biol Chem. 2003 Oct 3;278(40):39189-96
references.pmid: 12867417
references.citation: Microbiol Mol Biol Rev. 2006 Dec;70(4):910-38
references.pmid: 17158704
references.citation: J Biol Chem. 2008 May 16;283(20):13762-70
references.pmid: 18348979
references.citation: Acta Crystallogr D Biol Crystallogr. 1994 Jan 1;50(Pt 1):17-23
references.pmid: 15299472
references.citation: J Mol Biol. 1968 Apr 28;33(2):491-7
references.pmid: 5700707
references.citation: Mol Microbiol. 2012 Aug;85(3):535-56
references.pmid: 22676800
references.citation: Curr Opin Microbiol. 2010 Apr;13(2):232-9
references.pmid: 20138000
references.citation: J Bacteriol. 2010 Feb;192(4):1156-9
references.pmid: 20008068