2FA1
Crystal structure of PhnF C-terminal domain
2FA1 の概要
| エントリーDOI | 10.2210/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 | Lunin, V.V.,Nocek, B.P.,Gorelik, M.,Skarina, T.,Edwards, A.M.,Joachimiak, A.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2005-12-06, 公開日: 2006-01-10, 最終更新日: 2024-02-14) |
| 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: 16672238DOI: 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) |
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