2p6t

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spinqualitylabelsall models 2p6t, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF TRANSCRIPTIONAL REGULATOR NMB0573 and L-LEUCINE COMPLEX FROM NEISSERIA MENINGITIDIS

Overview

Neisseria meningitidis, a causative agent of bacterial meningitis, has a, relatively small repertoire of transcription factors, including NMB0573, (annotated AsnC), a member of the Lrp-AsnC family of regulators that are, widely expressed in both Bacteria and Archaea. In the present study we, show that NMB0573 binds to L-leucine and L-methionine and have solved the, structure of the protein with and without bound amino acids. This has, shown, for the first time that amino acid binding does not induce, significant conformational changes in the structure of an AsnC/Lrp, regulator though it does appear to stabilise the octameric assembly of the, protein. Transcriptional profiling of wild type and NMB0573 knock-out, strains of N. meningitidis has shown that NMB0573 is associated with an, adaptive response to nutrient poor conditions reflected in a reduction in, major surface protein expression. On the basis of its structure and the, transcriptional response, we propose that NMB0573 is a global regulator in, Neisseria controlling responses to nutrient availability through, indicators of general amino acid abundance; leucine and methionine.

About this Structure

2P6T is a Single protein structure of sequence from Neisseria meningitidis serogroup b with , and as ligands. Full crystallographic information is available from OCA.

Reference

The structure and transcriptional analysis of a global regulator from neisseria meningitidis., Ren J, Sainsbury S, Combs SE, Capper RG, Jordan PW, Berrow NS, Stammers DK, Saunders NJ, Owens RJ, J Biol Chem. 2007 Mar 20;. PMID:17374605

Page seeded by OCA on Wed Jan 23 15:05:24 2008