9XUZ
Solution structure of Site2 dimer of Ler
Summary for 9XUZ
| Entry DOI | 10.2210/pdb9xuz/pdb |
| Descriptor | Transcription regulator Ler (1 entity in total) |
| Functional Keywords | transcriptional regulator, dna binding protein, h-ns family, dimer, transcription |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 13941.49 |
| Authors | |
| Primary citation | Wang, G.,Duan, B.,Xia, B. Structural basis of the oligomerization of anti-silencer Ler from enterohemorrhagic E. coli (EHEC). Struct Dyn., 13:024702-024702, 2026 Cited by PubMed Abstract: The locus of enterocyte effacement-encoded regulator (Ler) is a master transcriptional activator essential for the virulence of enterohemorrhagic and enteropathogenic . Although Ler shares homology with the global silencer H-NS, it functions uniquely as an anti-silencer, a role strictly dependent on its oligomerization state. However, the structural mechanism governing Ler assembly remains poorly understood. In this study, we have characterized the N-terminal oligomerization domain (Ler) of Ler using solution NMR spectroscopy and biophysical assays, and found that Ler shows concentration-dependent oligomerization. We demonstrate that Ler oligomerization is driven by two distinct interfaces with contrasting dynamic properties. We determined the solution structure of the Ler dimer, revealing a stable, anti-parallel "tail-to-tail" interface (dimer Site-2, residues 35-66) stabilized by a hydrophobic core. In contrast, the N-terminal interface (dimer Site-1, residues 12-33) forms a highly dynamic "head-to-head" dimer, which undergoes significant conformational exchange and exhibits concentration- and temperature-dependent dimerization. Based on these findings, we propose a structural model wherein Ler forms supramolecular assemblies through the propagation of alternating stable (Site-2) and dynamic (Site-1) interactions. This architecture, while reminiscent of H-NS, displays distinct stability features that may underlie Ler's specific anti-silencing function in bacterial pathogenesis. PubMed: 41987883DOI: 10.1063/4.0001203 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
