2LPM

Chemical Shift and Structure Assignments for Sma0114

Summary for 2LPM

• Entry DOI: 10.2210/pdb2lpm/pdb
• NMR Information: BMRB: 16905
• Descriptor: Two-component response regulator (1 entity in total)
• Functional Keywords: transcription regulator
• Biological source: Sinorhizobium meliloti
• Total number of polymer chains: 1
• Total formula weight: 13606.51

Authors

Sheftic, S.R.,Gage, D.J.,Alexandrescu, A.T. (deposition date: 2012-02-15, release date: 2012-09-12, Last modification date: 2024-05-01)

Primary citation

Sheftic, S.R.,Garcia, P.P.,White, E.,Robinson, V.L.,Gage, D.J.,Alexandrescu, A.T.
Nuclear Magnetic Resonance Structure and Dynamics of the Response Regulator Sma0114 from Sinorhizobium meliloti.
Biochemistry, 51:6932-6941, 2012

PubMed Abstract: Receiver domains control intracellular responses triggered by signal transduction in bacterial two-component systems. Here, we report the solution nuclear magnetic resonance structure and dynamics of Sma0114 from the bacterium Sinorhizobium meliloti, the first such characterization of a receiver domain from the HWE-kinase family of two-component systems. The structure of Sma0114 adopts a prototypical α(5)/β(5) Rossman fold but has features that set it apart from other receiver domains. The fourth β-strand of Sma0114 houses a PFxFATGY sequence motif, common to many HWE-kinase-associated receiver domains. This sequence motif in Sma0114 may substitute for the conserved Y-T coupling mechanism, which propagates conformational transitions in the 455 (α4-β5-α5) faces of receiver domains, to prime them for binding downstream effectors once they become activated by phosphorylation. In addition, the fourth α-helix of the consensus 455 face in Sma0114 is replaced with a segment that shows high flexibility on the pico- to nanosecond time scale by (15)N relaxation data. Secondary structure prediction analysis suggests that the absence of helix α4 may be a conserved property of the HWE-kinase-associated family of receiver domains to which Sma0114 belongs. In spite of these differences, Sma0114 has a conserved active site, binds divalent metal ions such as Mg(2+) and Ca(2+) that are required for phosphorylation, and exhibits micro- to millisecond active-site dynamics similar to those of other receiver domains. Taken together, our results suggest that Sma0114 has a conserved active site but differs from typical receiver domains in the structure of the 455 face that is used to effect signal transduction following activation.

PubMed: 22880754
DOI: 10.1021/bi300922z

Experimental method

SOLUTION NMR