2oqr
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(New page: 200px<br /><applet load="2oqr" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oqr, resolution 2.030Å" /> '''The structure of th...)
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Revision as of 09:12, 23 January 2008
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The structure of the response regulator RegX3 from Mycobacterium tuberculosis
Overview
The full-length, two-domain response regulator RegX3 from Mycobacterium, tuberculosis is a dimer stabilised by 3D domain-swapping. Dimerisation is, known to occur in the OmpR/PhoB subfamily of response regulators upon, activation but has previously only been structurally characterised for, isolated receiver domains. The RegX3 dimer has a bipartite intermolecular, interface, which buries 2 357 A2 per monomer. The two parts of the, interface are between the two receiver domains (dimerisation interface), and between a composite receiver domain and the effector domain of the, second molecule (interdomain interface). The structure provides support, for the importance of threonine and tyrosine residues in the signal, transduction mechanism. These residues occur in an active-like, conformation stabilised by lanthanum ions. In solution RegX3 exists as, both a monomer and a dimer in a concentration-dependent equilibrium. The, dimer in solution differs from the active form observed in the crystal, resembling instead the model of the inactive full-length response, regulator PhoB.
About this Structure
2OQR is a Single protein structure of sequence from Mycobacterium tuberculosis with , and as ligands. Full crystallographic information is available from OCA.
Reference
The structure of a full-length response regulator from mycobacterium tuberculosis in a stabilised 3D domain-swapped, activated state., King-Scott J, Nowak E, Mylonas E, Panjikar S, Roessle M, Svergun DI, Tucker PA, J Biol Chem. 2007 Oct 16;. PMID:17942407
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