3FPV

Crystal Structure of HbpS

3FPV の概要

• エントリーDOI: 10.2210/pdb3fpv/pdb
• 関連するPDBエントリー: 3FPW
• 分子名称: Extracellular haem-binding protein, FE (III) ION (3 entities in total)
• 機能のキーワード: haem binding, heme binding protein
• 由来する生物種: Streptomyces reticuli
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 151816.53

構造登録者

Ortiz de Orue Lucana, D.,Bogel, G.,Zou, P.,Groves, M.R. (登録日: 2009-01-06, 公開日: 2009-01-20, 最終更新日: 2024-04-03)

主引用文献

Ortiz de Orue Lucana, D.,Bogel, G.,Zou, P.,Groves, M.R.
The oligomeric assembly of the novel haem-degrading protein HbpS is essential for interaction with its cognate two-component sensor kinase
J.Mol.Biol., 386:1108-1122, 2009

PubMed Abstract: HbpS, a novel protein of previously unknown function from Streptomyces reticuli, is up-regulated in response to haemin- and peroxide-based oxidative stress and interacts with the SenS/SenR two-component signal transduction system. In this study, we report the high-resolution crystal structures (2.2 and 1.6 A) of octomeric HbpS crystallized in the presence and in the absence of haem and demonstrate that iron binds to surface-exposed lysine residues of an octomeric assembly. Based on an analysis of the crystal structures, we propose that the iron atom originates from the haem group and report subsequent biochemical experiments that demonstrate that HbpS possesses haem-degrading activity in vitro. Further examination of the crystal structures has identified amino acids that are essential for assembly of the octomer. The role of these residues is confirmed by biophysical experiments. Additionally, we show that while the octomeric assembly state of HbpS is not essential for haem-degrading activity, the assembly of HbpS is required for its interaction with the cognate sensor kinase, SenS. Homologs of HbpS and SenS/SenR have been identified in a number of medically and ecologically relevant bacterial species (including Vibrio cholerae, Klebsiella pneumoniae, Corynebacterium diphtheriae, Arthrobacter aurescens and Pseudomonas putida), suggesting the existence of a previously undescribed bacterial oxidative stress-response pathway common to Gram-negative and Gram-positive bacteria. Thus, the data presented provide the first insight into the function of a novel protein family and an example of an iron-mediated interaction between an accessory protein and its cognate two-component sensor kinase.

PubMed: 19244623
DOI: 10.1016/j.jmb.2009.01.017

実験手法

X-RAY DIFFRACTION (2.2 Å)