3HHG: Structure Of Crga, A Lysr-Type Transcriptional Regulator From Neisseria Meningitidis

Citation:
Abstract
LysR-type transcriptional regulators (LTTRs) form the largest family of bacterial regulators acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes. The LTTR, CrgA, from the human pathogen Neisseria meningitidis, is upregulated during bacterial-host cell contact. Here, we report the crystal structures of both regulatory domain and full-length CrgA, the first of a novel subclass of LTTRs that form octameric rings. Non-denaturing mass spectrometry analysis and analytical ultracentrifugation established that the octameric form of CrgA is the predominant species in solution in both the presence and absence of an oligonucleotide encompassing the CrgA-binding sequence. Furthermore, analysis of the isolated CrgA-DNA complex by mass spectrometry showed stabilization of a double octamer species upon DNA binding. Based on the observed structure and the mass spectrometry findings, a model is proposed in which a hexadecameric array of two CrgA oligomers binds to its DNA target site.
PDB ID: 3HHGDownload
MMDB ID: 75176
PDB Deposition Date: 2009/5/15
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 3.2  Å
Source Organism:
Similar Structures:
Biological Unit for 3HHG: octameric; determined by author and by software (PISA)
Molecular Components in 3HHG
Label Count Molecule
Proteins (8 molecules)
8
Transcriptional Regulator, Lysr Family
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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