5LWK
MaeR response regulator bound to beryllium trifluoride
Summary for 5LWK
| Entry DOI | 10.2210/pdb5lwk/pdb |
| Descriptor | Transcriptional regulatory protein, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | response regulator beryllium trifluoride catalytic aspartic acid, transcription |
| Biological source | Lactobacillus paracasei |
| Total number of polymer chains | 2 |
| Total formula weight | 28371.20 |
| Authors | Miguel-Romero, L.,Casino, P.,Landete, J.M.,Monedero, V.,Zuniga, M.,Marina, A. (deposition date: 2016-09-18, release date: 2017-06-28, Last modification date: 2024-01-17) |
| Primary citation | Miguel-Romero, L.,Casino, P.,Landete, J.M.,Monedero, V.,Zuniga, M.,Marina, A. The malate sensing two-component system MaeKR is a non-canonical class of sensory complex for C4-dicarboxylates. Sci Rep, 7:2708-2708, 2017 Cited by PubMed Abstract: Microbial colonization of different environments is enabled to a great extent by the plasticity of their sensory mechanisms, among them, the two-component signal transduction systems (TCS). Here, an example of TCS plasticity is presented: the regulation of L-malate catabolism via malic enzyme by MaeRK in Lactobacillales. MaeKR belongs to the citrate family of TCS as the Escherichia coli DcuSR system. We show that the Lactobacillus casei histidine-kinase MaeK is defective in autophosphorylation activity as it lacks a functional catalytic and ATP binding domain. The cognate response regulator MaeR was poorly phosphorylated at its phosphoacceptor Asp in vitro. This phosphorylation, however, enhanced MaeR binding in vitro to its target sites and it was required for induction of regulated genes in vivo. Elucidation of the MaeR structure revealed that response regulator dimerization is accomplished by the swapping of α4-β5-α5 elements between two monomers, generating a phosphoacceptor competent conformation. Sequence and phylogenetic analyses showed that the MaeKR peculiarities are not exclusive to L. casei as they are shared by the rest of orthologous systems of Lactobacillales. Our results reveal MaeKR as a non-canonical TCS displaying distinctive features: a swapped response regulator and a sensor histidine kinase lacking ATP-dependent kinase activity. PubMed: 28577341DOI: 10.1038/s41598-017-02900-z PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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