The identification of metal-binding ligand residues in metalloproteins using nuclear magnetic resonance spectroscopy

Protein Science

Volumn 7, Issue 11, 1998, Pages 2476-2479

  Scrofani, Sergio D B ^a,b   Wright, Peter E ^a   Dyson, H Jane ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b Zenyth Therapeutics Limited Australia   (Australia)

Author keywords

Metal binding ligands; Metallo lactamase; Metalloprotein; NMR

Indexed keywords

BETA LACTAMASE; CADMIUM; CYSTEINE; HISTIDINE; LIGAND; METAL; METALLOPROTEIN; NITROGEN 15; PROTON;

ARTICLE; BACTEROIDES FRAGILIS; LIGAND BINDING; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL;

EID: 0031792029     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071128     Document Type: Article

References (18)

1. Baldwin GS, Galdes A, Hill HAO, Smith BE, Waley SG, Abraham EP. 1978. Histidine residues of zinc ligands in beta lactamase II. Biochem J 175:441-447.
2. 199Hg substituted P. furiosus rubredoxin: Implications for biological electron transfer. New J Chem 18:387-395.
3. Carfi A, Pares S, Duée E, Galleni M, Duez C, Frère JM, Dideberg O. 1995. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J 14:4914-4921.
4. Coleman JE. 1993. Cadmium-113 nuclear magnetic resonance applied to metalloproteins. Methods Enzymol 227:16-43.
5. Concha NO, Rasmussen BA, Bush K, Herzberg O. 1996. Crystal structure of the wide-spectrum β-lactamase from Bacteroides fragilis. Structure 4:823-836.
6. Crowder MW, Wang Z, Franklin S, Zovinka E, Que L Jr, Benkovic SJ. 1996. Characterization of the metal-binding sites of β-lactamase from Bacteroides fragilis. Biochemistry 35:12126-12132.
7. 113Cd heteronuclear two-dimensional NMR experiments. J Am Chem Soc 107:6847-6851.
8. 1H heteroTOCSY: A method for determining metal-protein connectivities. J Biomol NMR 4:761-774.
9. 13C magnetization. J Magn Reson Series B 101:114-119.
10. Grzesiek S, Bax A. 1992. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114:6291-6293.
11. Marion D, Ikura M, Tschudin R, Bax A. 1989. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Reson 85:393-399.
12. Payne DJ. 1993. Metallo-β-lactamases - A new therapeutic challenge. J Med Microbiol 39:93-99.
13. 15N NMR backbone assignments of 25.5 kDa metallo-β-lactamase from Bacteroides fragilis. J Biomol NMR 12:201-202.
14. 113Cd NMR studies of a 1:1 Cd adduct with an 18-residue finger peptide from HIV-1 nucleic acid binding protein, p7. J Am Chem Soc 111:395-392.
15. Sutton BJ, Artymiuk PJ, Cordera-Borboa AE, Little C, Phillips DC, Waley SG. 1987. An X-ray crystallographic study of β-lactamase II from Bacillus cereus at 0.35 Å resolution. Biochem J 245:181-188.
16. 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135-140.
17. Yang Y, Rasmussen BA, Bush K. 1992. Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636. Antimicrob Agents Chemother 56:1155-1157.
18. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J Biomol NMR 4:845-858.