2VHB

AZIDE ADDUCT OF THE BACTERIAL HEMOGLOBIN FROM VITREOSCILLA STERCORARIA

2VHB の概要

• エントリーDOI: 10.2210/pdb2vhb/pdb
• 分子名称: HEMOGLOBIN, AZIDE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: heme, respiratory protein, oxygen transport
• 由来する生物種: Vitreoscilla stercoraria
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32897.55

構造登録者

Tarricone, C.,Galizzi, A.,Coda, A.,Ascenzi, P.,Bolognesi, M. (登録日: 1997-02-19, 公開日: 1998-02-25, 最終更新日: 2024-02-21)

主引用文献

Tarricone, C.,Galizzi, A.,Coda, A.,Ascenzi, P.,Bolognesi, M.
Unusual structure of the oxygen-binding site in the dimeric bacterial hemoglobin from Vitreoscilla sp.
Structure, 5:497-507, 1997

PubMed Abstract: The first hemoglobin identified in bacteria was isolated from Vitreoscilla stercoraria (VtHb) as a homodimeric species. The wild-type protein has been reported to display medium oxygen affinity and cooperative ligand-binding properties. Moreover, VtHb can support aerobic growth in Escherichia coli with impaired terminal oxidase function. This ability of VtHb to improve the growth properties of E. coli has important applications in fermentation technology, assisting the overexpression of recombinant proteins and antibiotics. Oxygen binding heme domains have been identified in chimeric proteins from bacteria and yeast, where they are covalently linked to FAD- and NAD(P)H-binding domains. We investigate here the fold, the distal heme site structure and the quaternary assembly of a bacterial hemoglobin which does not bear the typical flavohemoglobin domain organization.

PubMed: 9115439
DOI: 10.1016/S0969-2126(97)00206-2

実験手法

X-RAY DIFFRACTION (1.76 Å)