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Structural characterization of GntR/HutC family signaling domain
Author(s) -
Gorelik Marina,
Lunin Vladimir V.,
Skarina Tatiana,
Savchenko Alexei
Publication year - 2006
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.062146906
Subject(s) - characterization (materials science) , domain (mathematical analysis) , chemistry , biology , computational biology , microbiology and biotechnology , nanotechnology , materials science , mathematics , mathematical analysis
The crystal structure of Escherichia coli PhnF C‐terminal domain (C‐PhnF) was solved at 1.7 Å resolution by the single wavelength anomalous dispersion (SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N‐terminal DNA‐binding domains, but are divided into four subfamilies according to their heterogenic C‐terminal domains, which are involved in effector binding and oligomerization. The C‐PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR‐like regulators. The structure represents a mixture of α‐helices and β‐strands, with a six‐stranded antiparallel β‐sheet at the core. C‐PhnF monomers form a dimer by establishing interdomain eight‐strand β‐sheets that include core antiparallel and N‐terminal two‐strand parallel β‐sheets from each monomer. C‐PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix‐turn‐helix loops. The structural comparison of the C‐PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding.