A backbone resonance assignment of the P24 fragment from S. aureus, complexed with novobiocin, was recently published. The assignment of fragment P24 in the apo form is not available, although this would be important to map the binding site of potential inhibitors. Moreover, all published crystallographic structures of inhibitors complexed with the P24 fragment are of the protein from E. coli for which NMR data have not been published. For these reasons, we decided to characterise the apo form of the 24 kDa N-terminal fragment of gyrase B from E. coli by NMR. Here, we report the assignment of backbone 1H, 15N, 13C and 13Cβ resonances of this protein. Besides being a useful tool to validate the crystallographic results, this work represents a first step toward an NMR-based procedure to design new antimicrobial agents targeted against DNA-gyrase.

Backbone 1H, 13C and 15N Resonance Assignment of the N-Terminal 24 kDa Fragment of the GyraseB Subunit from E. coli

BELLANDA, MASSIMO;PEGGION, EVARISTO;MAMMI, STEFANO
2002

Abstract

A backbone resonance assignment of the P24 fragment from S. aureus, complexed with novobiocin, was recently published. The assignment of fragment P24 in the apo form is not available, although this would be important to map the binding site of potential inhibitors. Moreover, all published crystallographic structures of inhibitors complexed with the P24 fragment are of the protein from E. coli for which NMR data have not been published. For these reasons, we decided to characterise the apo form of the 24 kDa N-terminal fragment of gyrase B from E. coli by NMR. Here, we report the assignment of backbone 1H, 15N, 13C and 13Cβ resonances of this protein. Besides being a useful tool to validate the crystallographic results, this work represents a first step toward an NMR-based procedure to design new antimicrobial agents targeted against DNA-gyrase.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/2461140
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