2FA1

Crystal structure of PhnF C-terminal domain

Summary for 2FA1

• Entry DOI: 10.2210/pdb2fa1/pdb
• Descriptor: Probable transcriptional regulator phnF, beta-D-fructopyranose (3 entities in total)
• Functional Keywords: pnhf, transcription, regulator, apc5558, effector binding domain, psi, protein structure initiative, mcsg, midwest center for structural genomics
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 36206.97

Authors

Lunin, V.V.,Nocek, B.P.,Gorelik, M.,Skarina, T.,Edwards, A.M.,Joachimiak, A.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2005-12-06, release date: 2006-01-10, Last modification date: 2024-02-14)

Primary citation

Gorelik, M.,Lunin, V.V.,Skarina, T.,Savchenko, A.
Structural characterization of GntR/HutC family signaling domain.
Protein Sci., 15:1-6, 2006

PubMed Abstract: The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 A 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 alpha-helices and beta-strands, with a six-stranded antiparallel beta-sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand beta-sheets that include core antiparallel and N-terminal two-strand parallel beta-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.

PubMed: 16672238
DOI: 10.1110/ps.062146906

Experimental method

X-RAY DIFFRACTION (1.7 Å)