1MU4

CRYSTAL STRUCTURE AT 1.8 ANGSTROMS OF THE BACILLUS SUBTILIS CATABOLITE REPRESSION HISTIDINE CONTAINING PROTEIN (CRH)

Summary for 1MU4

• Entry DOI: 10.2210/pdb1mu4/pdb
• Related: 1MO1
• Descriptor: HPr-like protein crh, SULFATE ION (3 entities in total)
• Functional Keywords: open-faced b-sandwich, phosphotransferase system, swapping domain, transport protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 19444.09

Authors

Juy, M.R.,Haser, R. (deposition date: 2002-09-23, release date: 2003-10-07, Last modification date: 2024-02-14)

Primary citation

Juy, M.R.,Penin, F.,Favier, A.,Galinier, A.,Montserret, R.,Haser, R.,Deutscher, J.,Bockmann, A.
Dimerization of Crh by reversible 3D Domain Swapping Induces Structural Adjustments to its monomeric homologue HPR
J.Mol.Biol., 332:767-776, 2003

PubMed Abstract: The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity.

PubMed: 12972249
DOI: 10.1016/S0022-2836(03)00918-5

Experimental method

X-RAY DIFFRACTION (1.8 Å)