Backbone resonance assignments; lysozyme; protein folding
Abstract :
[en] Lysozyme from lambda bacteriophage (lambda lysozyme) is an 18 kDa globular protein displaying some of the structural features common to all lysozymes; in particular, lambda lysozyme consists of two structural domains connected by a helix, and has its catalytic residues located at the interface between these two domains. An interesting feature of lambda lysozyme, when compared to the well-characterised hen egg-white lysozyme, is its lack of disulfide bridges; this makes lambda lysozyme an interesting system for studies of protein folding. A comparison of the folding properties of lambda lysozyme and hen lysozyme will provide important insights into the role that disulfide bonds play in the refolding pathway of the latter protein. Here we report the (1)H, (13)C and (15)N backbone resonance assignments for lambda lysozyme by heteronuclear multidimensional NMR spectroscopy. These assignments provide the starting point for detailed investigation of the refolding pathway using pulse-labelling hydrogen/deuterium exchange experiments monitored by NMR.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Di Paolo, Alexandre ; Université de Liège - ULiège > Sciences de la Vie > Enzymologie et Repliement des Protéine, Centre d'ingénierie des protéines
Duval, Valerie; Université de Liège - ULiège > Centre d'ingénierie des protéines
Matagne, André ; Université de Liège - ULiège > Département des sciences de la vie > Enzymologie et repliement des protéines
Redfield, Christina; University of Oxford > Department of Biochemistry
Language :
English
Title :
Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.
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Bibliography
CM Dobson PA Evans SE Radford 1994 Understanding how proteins fold: the lysozyme story so far Trends Biochem Sci 19 31 37 10.1016/0968-0004(94)90171-6 (Pubitemid 24028729)
C Evrard J Fastrez JP Declercq 1998 Crystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes J Mol Biol 276 151 164 10.1006/jmbi.1997.1499 (Pubitemid 28085415)
MJ Gething J Sambrook 1992 Protein folding in the cell Nature 355 33 45 10.1038/355033a0 1992Natur.355...33G
ME Goldberg R Rudolph R Jaenicke 1991 A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme Biochemistry 30 2790 2797 10.1021/bi00225a008
R Kuroki LH Weaver BW Matthews 1995 Structure-based design of a lysozyme with altered catalytic activity Nat Struct Biol 2 1007 1011 10.1038/nsb1195-1007
AK Leung HS Duewel JF Honek AM Berghuis 2001 Crystal structure of the lytic transglycosylase from bacteriophage lambda in complex with hexa-N-acetylchitohexaose Biochemistry 40 5665 5673 10.1021/bi0028035 (Pubitemid 32440870)
A Matagne CM Dobson 1998 The folding process of hen lysozyme: a perspective from the 'new view' Cell Mol Life Sci 54 363 371 10.1007/s000180050165 (Pubitemid 28192744)
A Matagne M Jamin EW Chung CV Robinson SE Radford CM Dobson 2000 Thermal unfolding of an intermediate is associated with non-Arrhenius kinetics in the folding of hen lysozyme J Mol Biol 297 193 210 10.1006/jmbi.2000.3540
BW Matthews 1996 Structural and genetic analysis of the folding and function of T4 lysozyme Faseb J 10 35 41 (Pubitemid 26035504)
BW Matthews SJ Remington MG Grutter WF Anderson 1981 Relation between hen egg white lysozyme and bacteriophage T4 lysozyme: evolutionary implications J Mol Biol 147 545 558 10.1016/0022-2836(81)90399-5 (Pubitemid 11082559)
A Miranker CV Robinson SE Radford RT Aplin CM Dobson 1993 Detection of transient protein folding populations by mass spectrometry Science 262 896 900 10.1126/science.8235611 1993Sci...262..896M (Pubitemid 24014076)
SE Radford CM Dobson PA Evans 1992 The folding of hen lysozyme involves partially structured intermediates and multiple pathways Nature 358 302 307 10.1038/358302a0 1992Natur.358..302R
B van den Berg EW Chung CV Robinson CM Dobson 1999 Characterisation of the dominant oxidative folding intermediate of hen lysozyme J Mol Biol 290 781 796 10.1006/jmbi.1999.2915 (Pubitemid 29355707)
DS Wishart BD Sykes 1994 The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data J Biomol NMR 4 171 180 10.1007/BF00175245
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