3HYJ

Crystal structure of the N-terminal LAGLIDADG domain of DUF199/WhiA

Summary for 3HYJ

• Entry DOI: 10.2210/pdb3hyj/pdb
• Related: 3HYI
• Descriptor: Protein DUF199/WhiA, GLYCEROL, SODIUM ION, ... (5 entities in total)
• Functional Keywords: laglidadg, homing endonuclease, helix-turn-helix, hth, transcription regulator
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 46472.12

Authors

Kaiser, B.K.,Clifton, M.C.,Shen, B.W.,Stoddard, B.L. (deposition date: 2009-06-22, release date: 2009-09-01, Last modification date: 2024-02-21)

Primary citation

Kaiser, B.K.,Clifton, M.C.,Shen, B.W.,Stoddard, B.L.
The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease.
Structure, 17:1368-1376, 2009

PubMed Abstract: Proteins of the DUF199 family, present in all Gram-positive bacteria and best characterized by the WhiA sporulation control factor in Streptomyces coelicolor, are thought to act as genetic regulators. The crystal structure of the DUF199/WhiA protein from Thermatoga maritima demonstrates that these proteins possess a bipartite structure, in which a degenerate N-terminal LAGLIDADG homing endonuclease (LHE) scaffold is tethered to a C-terminal helix-turn-helix (HTH) domain. The LHE domain has lost those residues critical for metal binding and catalysis, and also displays an extensively altered DNA-binding surface as compared with homing endonucleases. The HTH domain most closely resembles related regions of several bacterial sigma70 factors that bind the -35 regions of bacterial promoters. The structure illustrates how an invasive element might be transformed during evolution into a larger assemblage of protein folds that can participate in the regulation of a complex biological pathway.

PubMed: 19836336
DOI: 10.1016/j.str.2009.08.008

Experimental method

X-RAY DIFFRACTION (2.6 Å)