Localising individual atoms of tryptophan side chains in the metallo-β-lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites
Henry W. Orton,Iresha D. Herath,Ansis Maleckis,Shereen Jabar,Monika Szabo,Bim Graham,Colum Breen,Lydia Topping,Stephen J. Butler,and Gottfried Otting
ARC Centre of Excellence for Innovations in Peptide & Protein
Science, Research School of Chemistry, Australian National University,
Canberra, ACT 2601, Australia
Iresha D. Herath
Research School of Chemistry, The Australian National University,
Sullivans Creek Road, Canberra ACT 2601, Australia
Ansis Maleckis
Latvian Institute of Organic Synthesis, Aizkraukles 21, 1006 Riga,
Latvia
Shereen Jabar
Research School of Chemistry, The Australian National University,
Sullivans Creek Road, Canberra ACT 2601, Australia
Monika Szabo
Monash Institute of Pharmaceutical Sciences, Monash University,
Parkville, VIC 3052, Australia
Bim Graham
Monash Institute of Pharmaceutical Sciences, Monash University,
Parkville, VIC 3052, Australia
Colum Breen
Department of Chemistry, Loughborough University, Epinal Way, Loughborough, LE11 3TU, United Kingdom
Lydia Topping
Department of Chemistry, Loughborough University, Epinal Way, Loughborough, LE11 3TU, United Kingdom
Stephen J. Butler
Department of Chemistry, Loughborough University, Epinal Way, Loughborough, LE11 3TU, United Kingdom
ARC Centre of Excellence for Innovations in Peptide & Protein
Science, Research School of Chemistry, Australian National University,
Canberra, ACT 2601, Australia
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This paper explores a method for determining the solution structure of a solvent-exposed polypeptide segment (the L3 loop), which is next to the active site of the penicillin-degrading enzyme IMP-1. Tagging three different sites on the protein with paramagnetic metal ions allowed positioning of the L3 loop with atomic resolution. It was found that the method was more robust when omitting data obtained with different metal ions if obtained with the same tag at the same tagging site.
This paper explores a method for determining the solution structure of a solvent-exposed...
