6lxm

Crystal structure of C-terminal DNA-binding domain of Escherichia coli OmpR as a domain-swapped dimerCrystal structure of C-terminal DNA-binding domain of Escherichia coli OmpR as a domain-swapped dimer

Structural highlights 6lxm is a 3 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.412Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function OMPR_ECOLI The N-terminus of this protein is required for the transcriptional expression of both major outer membrane protein genes ompF and ompC; its C-terminal moiety mediates the multimerization of the OmpR protein. As a multimer, it turns on the expression of the ompC gene; as a monomer, it turns on the expression of the ompF gene.

spinqualitylabelsall models 6lxm, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image