1tlv

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spinqualitylabelsall models 1tlv, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of the native and inactive LicT PRD from B. subtilis

Overview

The transcriptional antiterminator protein LicT regulates the expression, of Bacillus subtilis operons involved in beta-glucoside metabolism. It, consists of an N-terminal RNA-binding domain (co-antiterminator (CAT)) and, two phosphorylatable phosphotransferase system regulation domains (PRD1, and PRD2). In the activated state, each PRD forms a dimeric unit with the, phosphorylation sites totally buried at the dimer interface. Here we, present the 1.95 A resolution structure of the inactive LicT PRDs as well, as the molecular solution structure of the full-length protein deduced, from small angle x-ray scattering. Comparison of native (inactive) and, mutant (constitutively active) PRD crystal structures shows massive, tertiary and quaternary rearrangements of the entire regulatory domain. In, the inactive state, a wide swing movement of PRD2 results in dimer opening, and brings the phosphorylation sites to the protein surface. This movement, is accompanied by additional structural rearrangements of both the, PRD1-PRD1 ' interface and the CAT-PRD1 linker. Small angle x-ray, scattering experiments indicate that the amplitude of the PRD2 swing might, even be wider in solution than in the crystals. Our results suggest that, PRD2 is highly mobile in the native protein, whereas it is locked upon, activation by phosphorylation.

About this Structure

1TLV is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes., Graille M, Zhou CZ, Receveur-Brechot V, Collinet B, Declerck N, van Tilbeurgh H, J Biol Chem. 2005 Apr 15;280(15):14780-9. Epub 2005 Feb 7. PMID:15699035

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