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Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase

dc.contributor.authorBiswas, Tapanen_US
dc.contributor.authorTsodikov, Oleg V.en_US
dc.date.accessioned2010-06-01T21:37:11Z
dc.date.available2010-06-01T21:37:11Z
dc.date.issued2008-06en_US
dc.identifier.citationBiswas, Tapan; Tsodikov, Oleg V. (2008). "Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase." FEBS Journal 275(12): 3064-3071. <http://hdl.handle.net/2027.42/74669>en_US
dc.identifier.issn1742-464Xen_US
dc.identifier.issn1742-4658en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/74669
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=18479467&dopt=citationen_US
dc.format.extent813980 bytes
dc.format.extent3109 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rightsJournal compilation © 2008 Federation of European Biochemical Societiesen_US
dc.subject.otherCrystal Structureen_US
dc.subject.otherDnaB Helicaseen_US
dc.subject.otherPrimaseen_US
dc.subject.otherReplicationen_US
dc.subject.otherTuberculosisen_US
dc.titleHexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicaseen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.identifier.pmid18479467en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/74669/1/j.1742-4658.2008.06460.x.pdf
dc.identifier.doi10.1111/j.1742-4658.2008.06460.xen_US
dc.identifier.sourceFEBS Journalen_US
dc.identifier.citedreferenceHirota Y, Ryter A & Jacob F ( 1968 ) Thermosensitive mutants of E. coli affected in the processes of DNA synthesis and cellular division. Cold Spring Harb Symp Quant Biol 33, 677 – 693.en_US
dc.identifier.citedreferenceLeBowitz JH & McMacken R ( 1986 ) The Escherichia coli dnaB replication protein is a DNA helicase. J Biol Chem 261, 4738 – 4748.en_US
dc.identifier.citedreferenceBaker TA, Sekimizu K, Funnell BE & Kornberg A ( 1986 ) Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome. Cell 45, 53 – 64.en_US
dc.identifier.citedreferenceSchaeffer PM, Headlam MJ & Dixon NE ( 2005 ) Protein–protein interactions in the eubacterial replisome. IUBMB Life 57, 5 – 12.en_US
dc.identifier.citedreferenceCorn JE & Berger JM ( 2006 ) Regulation of bacterial priming and daughter strand synthesis through helicase–primase interactions. Nucleic Acids Res 34, 4082 – 4088.en_US
dc.identifier.citedreferenceKaplan DL ( 2000 ) The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase. J Mol Biol 301, 285 – 299.en_US
dc.identifier.citedreferenceGalletto R, Jezewska MJ & Bujalowski W ( 2004 ) Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: quantitative analysis of the rate of the dsDNA unwinding, processivity and kinetic step-size of the Escherichia coli DnaB helicase using rapid quench-flow method. J Mol Biol 343, 83 – 99.en_US
dc.identifier.citedreferenceMok M & Marians KJ ( 1987 ) The Escherichia coli preprimosome and DNA B helicase can form replication forks that move at the same rate. J Biol Chem 262, 16644 – 16654.en_US
dc.identifier.citedreferenceTanner NA, Hamdan SM, Jergic S, Schaeffer PM, Dixon NE & van Oijen AM ( 2008 ) Single-molecule studies of fork dynamics in Escherichia coli DNA replication. Nat Struct Mol Biol 15, 170 – 176.en_US
dc.identifier.citedreferenceBailey S, Eliason WK & Steitz TA ( 2007 ) The crystal structure of the Thermus aquaticus DnaB helicase monomer. Nucleic Acids Res 35, 4728 – 4736.en_US
dc.identifier.citedreferenceBiswas SB, Chen PH & Biswas EE ( 1994 ) Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity. Biochemistry 33, 11307 – 11314.en_US
dc.identifier.citedreferenceWang G, Klein MG, Tokonzaba E, Zhang Y, Holden LG & Chen XS ( 2008 ) The structure of a DnaB-family replicative helicase and its interactions with primase. Nat Struct Mol Biol 15, 94 – 100.en_US
dc.identifier.citedreferenceBird LE, Pan H, Soultanas P & Wigley DB ( 2000 ) Mapping protein–protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry 39, 171 – 182.en_US
dc.identifier.citedreferenceBailey S, Eliason WK & Steitz TA ( 2007 ) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 318, 459 – 463.en_US
dc.identifier.citedreferenceSingleton MR, Sawaya MR, Ellenberger T & Wigley DB ( 2000 ) Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101, 589 – 600.en_US
dc.identifier.citedreferenceOakley AJ, Loscha KV, Schaeffer PM, Liepinsh E, Pintacuda G, Wilce MC, Otting G & Dixon NE ( 2005 ) Crystal and solution structures of the helicase-binding domain of Escherichia coli primase. J Biol Chem 280, 11495 – 11504.en_US
dc.identifier.citedreferenceLu YB, Ratnakar PV, Mohanty BK & Bastia D ( 1996 ) Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA. Proc Natl Acad Sci USA 93, 12902 – 12907.en_US
dc.identifier.citedreferenceThirlway J, Turner IJ, Gibson CT, Gardiner L, Brady K, Allen S, Roberts CJ & Soultanas P ( 2004 ) DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings. Nucleic Acids Res 32, 2977 – 2986.en_US
dc.identifier.citedreferenceLeipe DD, Aravind L, Grishin NV & Koonin EV ( 2000 ) The bacterial replicative helicase DnaB evolved from a RecA duplication. Genome Res 10, 5 – 16.en_US
dc.identifier.citedreferenceKaplan DL & O’Donnell M ( 2002 ) DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol Cell 10, 647 – 657.en_US
dc.identifier.citedreferenceSan Martin MC, Stamford NP, Dammerova N, Dixon NE & Carazo JM ( 1995 ) A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J Struct Biol 114, 167 – 176.en_US
dc.identifier.citedreferenceTsodikov OV, Record MT Jr & Sergeev YV ( 2002 ) Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature. J Comput Chem 23, 600 – 609.en_US
dc.identifier.citedreferenceThirlway J & Soultanas P ( 2006 ) In the Bacillus stearothermophilus DnaB–DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues. J Bacteriol 188, 1534 – 1539.en_US
dc.identifier.citedreferenceStordal L & Maurer R ( 1996 ) Defect in general priming conferred by linker region mutants of Escherichia coli dnaB. J Bacteriol 178, 4620 – 4627.en_US
dc.identifier.citedreferenceMiles CS, Weigelt J, Stamford NP, Dammerova N, Otting G & Dixon NE ( 1997 ) Precise limits of the N-terminal domain of DnaB helicase determined by NMR spectroscopy. Biochem Biophys Res Commun 231, 126 – 130.en_US
dc.identifier.citedreferenceSyson K, Thirlway J, Hounslow AM, Soultanas P & Waltho JP ( 2005 ) Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation. Structure 13, 609 – 616.en_US
dc.identifier.citedreferenceFass D, Bogden CE & Berger JM ( 1999 ) Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 7, 691 – 698.en_US
dc.identifier.citedreferenceWeigelt J, Brown SE, Miles CS, Dixon NE & Otting G ( 1999 ) NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure 7, 681 – 690.en_US
dc.identifier.citedreferenceSu XC, Schaeffer PM, Loscha KV, Gan PH, Dixon NE & Otting G ( 2006 ) Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase. FEBS J 273, 4997 – 5009.en_US
dc.identifier.citedreferenceTougu K & Marians KJ ( 1996 ) The extreme C terminus of primase is required for interaction with DnaB at the replication fork. J Biol Chem 271, 21391 – 21397.en_US
dc.identifier.citedreferenceChang P & Marians KJ ( 2000 ) Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork. J Biol Chem 275, 26187 – 26195.en_US
dc.identifier.citedreferenceLuft JR, Collins RJ, Fehrman NA, Lauricella AM, Veatch CK & DeTitta GT ( 2003 ) A deliberate approach to screening for initial crystallization conditions of biological macromolecules. J Struct Biol 142, 170 – 179.en_US
dc.identifier.citedreferenceOtwinowski Z & Minor W ( 1997 ) Processing of X-ray diffraction data collected in oscillation mode. Macromolec Crystallogr A 276, 307 – 326.en_US
dc.identifier.citedreferenceYeates TO ( 1997 ) Detecting and overcoming crystal twinning. Methods Enzymol 276, 344 – 358.en_US
dc.identifier.citedreferenceMccoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC & Read RJ ( 2007 ) Phaser crystallographic software. J Appl Crystallogr 40, 658 – 674.en_US
dc.identifier.citedreferenceEmsley P & Cowtan K ( 2004 ) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126 – 2132.en_US
dc.identifier.citedreferenceMurshudov GN, Vagin AA & Dodson EJ ( 1997 ) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53, 240 – 255.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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