title: Crystallization and preliminary X-ray diffraction analysis of the α subdomain of Lon protease from Brevibacillus thermoruber.
abstract: DNA-binding ability has previously been reported as a novel function for the thermostable Lon protease from Brevibacillus thermoruber WR-249 (Bt-Lon), and the α subdomain (amino acids 491-605) of Bt-Lon has been identified as being responsible for DNA binding. However, the physiological role and DNA-recognition mode of Bt-Lon still remain unclear. In this study, the crystallization and preliminary crystallographic analysis of the Bt-Lon α subdomain are presented. Native diffraction data to 2.88 Å resolution were obtained from a vitrified crystal at 100 K on the BL13C1 beamline at the NSRRC (National Synchrotron Radiation Research Center), Taiwan. The crystals belonged to space group P23, with unit-cell parameters a = b = c = 94.28 Å. Solvent-content calculations and molecular-replacement results suggest that there are two molecules of Bt-Lon α subdomain per asymmetric unit.
authors.affiliation: Department of Agricultural Chemistry, National Taiwan University, Taipei 10617, Taiwan.
authors.forename: Yu-Da
authors.initials: YD
authors.lastname: Chen
authors.forename: Yu-Yung
authors.initials: YY
authors.lastname: Chang
authors.forename: Shih-Hsiung
authors.initials: SH
authors.lastname: Wu
authors.forename: Chun-Hua
authors.initials: CH
authors.lastname: Hsu
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D058675:Brevibacillus / Q000201:enzymology*; D003460:Crystallization; D049070:Protease La / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D049070:Protease La
keywords: Brevibacillus thermoruber; DNA binding; Lon protease
references.citation: Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11247-51
references.pmid: 8248235
references.citation: Genome Res. 1999 Jan;9(1):27-43
references.pmid: 9927482
references.citation: Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21
references.pmid: 9757107
references.citation: J Mol Biol. 2010 Aug 27;401(4):653-70
references.pmid: 20600124
references.citation: Methods Enzymol. 1997;276:307-26
references.pmid: 27754618
references.citation: J Biol Chem. 2004 Aug 13;279(33):34903-12
references.pmid: 15181012
references.citation: J Biol Chem. 1994 Jan 7;269(1):238-42
references.pmid: 8276800
references.citation: FEBS Lett. 2002 Aug 28;526(1-3):66-70
references.pmid: 12208506
references.citation: Mol Endocrinol. 2007 Sep;21(9):2164-77
references.pmid: 17579211
references.citation: Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):195-7
references.pmid: 20124721
references.citation: Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6678-82
references.pmid: 10359771
references.citation: Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):355-67
references.pmid: 21460454
references.citation: Methods Enzymol. 1994;244:350-75
references.pmid: 7845219
references.citation: J Bacteriol. 1994 Nov;176(21):6528-37
references.pmid: 7961403
references.citation: Biochemistry. 2001 Aug 7;40(31):9317-23
references.pmid: 11478899
references.citation: J Bacteriol. 2002 Jul;184(13):3689-98
references.pmid: 12057965
references.citation: Biochem Biophys Res Commun. 2009 Oct 9;388(1):62-6
references.pmid: 19643080
references.citation: Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6787-90
references.pmid: 10359790
references.citation: Biochem J. 2001 Sep 1;358(Pt 2):473-80
references.pmid: 11513747
references.citation: Annu Rev Genet. 1996;30:465-506
references.pmid: 8982462
references.citation: J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
references.pmid: 19461840
references.citation: J Mol Biol. 1968 Apr 28;33(2):491-7
references.pmid: 5700707
references.citation: Proc Natl Acad Sci U S A. 1981 Apr;78(4):2043-7
references.pmid: 6264459