2iwb

From Proteopedia

Revision as of 15:12, 30 October 2007

MECR1 UNBOUND EXTRACELLULAR ANTIBIOTIC-SENSOR DOMAIN.

Overview

Methicillin-resistant Staphylococcus aureus (MRSA) strains are responsible, for most hospital-onset bacterial infections. Lately, they have become a, major threat to the community through infections of skin, soft tissue and, respiratory tract, and subsequent septicaemia or septic shock. MRSA, strains are resistant to most beta-lactam antibiotics (BLAs) as a result, of the biosynthesis of a penicillin-binding protein with low affinity for, BLAs, called PBP2a, PBP2' or MecA. This response is regulated by the, chromosomal mec-divergon, which encodes a signal-transduction system, including a transcriptional repressor, MecI, and a sensor/transducer, MecR1, as well as the structural mecA gene. This system is similar to, those encoded by bla divergons in S. aureus and Bacillus licheniformis., ... [(full description)]

About this Structure

2IWB is a [Single protein] structure of sequence from [Staphylococcus aureus] with NI and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Unbound and acylated structures of the MecR1 extracellular antibiotic-sensor domain provide insights into the signal-transduction system that triggers methicillin resistance., Marrero A, Mallorqui-Fernandez G, Guevara T, Garcia-Castellanos R, Gomis-Ruth FX, J Mol Biol. 2006 Aug 18;361(3):506-21. Epub 2006 Jul 7. PMID:16846613

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