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PDBsum entry 3hyj
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Transcription regulator
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PDB id
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3hyj
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References listed in PDB file
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Key reference
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Title
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The structure of a bacterial duf199/whia protein: domestication of an invasive endonuclease.
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Authors
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B.K.Kaiser,
M.C.Clifton,
B.W.Shen,
B.L.Stoddard.
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Ref.
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Structure, 2009,
17,
1368-1376.
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PubMed id
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Abstract
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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.
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