Catalytic break-down of beta-lactam antibiotics

Angewandte Chemie (International ed. in English)
Iron(III) located in the dinuclear metallo-β-lactamase IMP-1 by pseudocontact shifts.

Sample included an N-terminal expression tag (MASMTG) without the transport peptide
Residues -4 to 1 (MASMTG) represent a non-native T7 expression tag used for improved protein production yields in cell-free protein synthesis

IMP-1 peptide without the N-terminal signal peptide but with an N-terminal expression tag (MASMTG)

Iron ion bound by His77, His79, and His139

Zinc ion bound by Asp81, Cys158, and His197

Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa In Complex With A Mercaptocarboxylate Inhibitor

Crystal Structure Of Imp-1 Metallo Beta-lactamase From Pseudomonas Aeruginosa

Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa In Complex With A Biaryl Succinic Acid Inhibitor (11)

Imp-1 Metallo Beta-lactamase From Pseudomonas Aeruginosa In Complex With A Biaryl Succinic Acid Inhibitor (1)

Structure-Based Design Of The Irreversible Inhibitors To Metallo--Lactamase (Imp-1)

Crystal Structure Of Metallo-beta-lactamase Imp-1 Mutant (d81a)

Crystal Structure Of Metallo-Beta-Lactamase Imp-1 Mutant (D81e)

The Structure Of Imp-1 Complexed With The Detecting Reagent (Dansylc4sh) By A Fluorescent Probe

Crystal Structure Of Imp-1 Metallo-beta-lactamase Complexed With A 3- Aminophtalic Acid Inhibitor

Crystal Structure Of The Metallo-beta-lactamase Imp-1 With L-captopril

Crystal Structure Of The Metallo-beta-lactamase Imp-1 With D-captopril

Mutagenesis Of Zinc Ligand Residue Cys221 Reveals Plasticity In The Imp-1 Metallo-b-lactamase Active Site

1.8 Angstrom Crystal Structure Of Imp-1 Metallo-beta-lactamase With A Mixed Iron-zinc Center In The Active Site

metallo beta-lactamase [Klebsiella pneumoniae]

metallo-beta-lactamase [Serratia marcescens]

extended-spectrum B-lactamase [Pseudomonas aeruginosa]

metallo-beta lactamase [Serratia marcescens]

metallo-beta-lactamase IMP-1 [Acinetobacter baumannii]

metallo-beta-lactamase IMP-1 [Pseudomonas putida]

metallo beta-lactamase [Serratia marcescens]

IMP-1 metallo-beta-lactamase [Serratia marcescens]

beta-lactamase IMP-1 [Acinetobacter sp. A1411]

metallo-beta-lactamase IMP-1 [Pseudomonas aeruginosa]

MULTISPECIES: carbapenem-hydrolyzing metallo-beta-lactamase IMP-1 [Proteobacteria]

carbapenem-hydrolyzing metallo-beta-lactamase IMP-10 [Pseudomonas aeruginosa]

MULTISPECIES: carbapenem-hydrolyzing metallo-beta-lactamase IMP-6 [Gammaproteobacteria]

carbapenem-hydrolyzing metallo-beta-lactamase IMP-34 [Klebsiella oxytoca]

subclass B1 metallo-beta-lactamase, partial [Acinetobacter baumannii]

RecName: Full=Beta-lactamase IMP-1; AltName: Full=BLAIMP; AltName: Full=Beta-lactamase type II; AltName: Full=Penicillinase; Fl

The chemical shift assignments of [FeZn]-IMP-1 metallo-beta-lactamase.
The backbone chemical shift assignments of [FeZn]-IMP-1 metallo-beta-lactamase

Research School of Chemistry, Australian National University

Proton optimised triple resonance NMR cryoprobe

The chemical shift assignments of [ZnZn]-IMP-1 metallo-beta-lactamase.

Recombinant uniformly 13C/15N-labelled protein expressed in vivo

20 mM MES (pH 6.5), 100 mM NaCl, in a standard 5 mm tube

The CCPN NMR assignment and data analysis application

Bruker Topspin NMR acquistion and analysis application

NMRPipe Spectral Processing and Analysis System

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax

Bruker Pty. Ltd., Billerica, Massachusetts, USA

Department of Biochemistry, Cambridge CB2 1GA, UK