7DVV

Heme sensor protein PefR from Streptococcus agalactiae bound to operator DNA (28-mer)

7DVV の概要

• エントリーDOI: 10.2210/pdb7dvv/pdb
• 関連するPDBエントリー: 7DVR 7DVS 7DVT 7DVU
• 分子名称: HTH marR-type domain-containing protein, DNA (28-MER), ... (4 entities in total)
• 機能のキーワード: heme-binding, helix-turn-helix, transcription
• 由来する生物種: Streptococcus agalactiae serotype III (strain NEM316); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 52838.91

構造登録者

Nishinaga, M.,Nagai, S.,Nishitani, Y.,Sugimoto, H.,Shiro, Y.,Sawai, H. (登録日: 2021-01-15, 公開日: 2021-09-29, 最終更新日: 2023-11-29)

主引用文献

Nishinaga, M.,Sugimoto, H.,Nishitani, Y.,Nagai, S.,Nagatoishi, S.,Muraki, N.,Tosha, T.,Tsumoto, K.,Aono, S.,Shiro, Y.,Sawai, H.
Heme controls the structural rearrangement of its sensor protein mediating the hemolytic bacterial survival.
Commun Biol, 4:467-467, 2021

PubMed Abstract: Hemes (iron-porphyrins) are critical for biological processes in all organisms. Hemolytic bacteria survive by acquiring b-type heme from hemoglobin in red blood cells from their animal hosts. These bacteria avoid the cytotoxicity of excess heme during hemolysis by expressing heme-responsive sensor proteins that act as transcriptional factors to regulate the heme efflux system in response to the cellular heme concentration. Here, the underlying regulatory mechanisms were investigated using crystallographic, spectroscopic, and biochemical studies to understand the structural basis of the heme-responsive sensor protein PefR from Streptococcus agalactiae, a causative agent of neonatal life-threatening infections. Structural comparison of heme-free PefR, its complex with a target DNA, and heme-bound PefR revealed that unique heme coordination controls a >20 Å structural rearrangement of the DNA binding domains to dissociate PefR from the target DNA. We also found heme-bound PefR stably binds exogenous ligands, including carbon monoxide, a by-product of the heme degradation reaction.

PubMed: 33850260
DOI: 10.1038/s42003-021-01987-5

実験手法

X-RAY DIFFRACTION (2.49 Å)