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2FA1

Crystal structure of PhnF C-terminal domain

2FA1 の概要
エントリーDOI10.2210/pdb2fa1/pdb
分子名称Probable transcriptional regulator phnF, beta-D-fructopyranose (3 entities in total)
機能のキーワードpnhf, transcription, regulator, apc5558, effector binding domain, psi, protein structure initiative, mcsg, midwest center for structural genomics
由来する生物種Escherichia coli
タンパク質・核酸の鎖数2
化学式量合計36206.97
構造登録者
主引用文献Gorelik, M.,Lunin, V.V.,Skarina, T.,Savchenko, A.
Structural characterization of GntR/HutC family signaling domain.
Protein Sci., 15:1-6, 2006
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 2fa1
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-25に公開中

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