1S66

Crystal structure of heme domain of direct oxygen sensor from E. coli

1S66 の概要

• エントリーDOI: 10.2210/pdb1s66/pdb
• 分子名称: Hypothetical protein yddU, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total)
• 機能のキーワード: pas, oxygen sensor, dos, heme protein, oxygen storage-transport complex, oxygen storage/transport
• 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: 28413.95

構造登録者

Park, H.J.,Suquet, C.,Satterlee, J.D.,Kang, C.H. (登録日: 2004-01-22, 公開日: 2004-06-22, 最終更新日: 2024-02-14)

主引用文献

Park, H.J.,Suquet, C.,Satterlee, J.D.,Kang, C.H.
Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH)
Biochemistry, 43:2738-2746, 2004

PubMed Abstract: The X-ray crystal structure of the Escherichia coli (Ec) direct oxygen sensor heme domain (Ec DosH) has been solved to 1.8 A using Fe multiple-wavelength anomalous dispersion (MAD), and the positions of Met95 have been confirmed by selenomethionine ((Se)Met) MAD. Ec DosH is the sensing part of a larger two-domain sensing/signaling protein, in which the signaling domain has phosphodiesterase activity. The asymmetric unit of the crystal lattice contains a dimer comprised of two differently ligated heme domain monomers. Except for the heme ligands, the monomer heme domains are identical. In one monomer, the heme is ligated by molecular oxygen (O(2)), while in the other monomer, an endogenous Met95 with S --> Fe ligation replaces the exogenous O(2) ligand. In both heme domains, the proximal ligand is His77. Analysis of these structures reveals sizable ligand-dependent conformational changes in the protein chain localized in the FG turn, the G(beta)-strand, and the HI turn. These changes provide insight to the mechanism of signal propagation within the heme domain following initiation due to O(2) dissociation.

PubMed: 15005609
DOI: 10.1021/bi035980p

実験手法

X-RAY DIFFRACTION (1.8 Å)