3hyj
Crystal structure of the N-terminal LAGLIDADG domain of DUF199/WhiACrystal structure of the N-terminal LAGLIDADG domain of DUF199/WhiA
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedProteins 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. The structure of a bacterial DUF199/WhiA protein: domestication of an invasive endonuclease.,Kaiser BK, Clifton MC, Shen BW, Stoddard BL Structure. 2009 Oct 14;17(10):1368-76. PMID:19836336[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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