1KR7

Crystal structure of the nerve tissue mini-hemoglobin from the nemertean worm Cerebratulus lacteus

1KR7 の概要

• エントリーDOI: 10.2210/pdb1kr7/pdb
• 分子名称: Neural globin, SULFATE ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: nerve tissue, mini-hemoglobin, protein cavities, oxygen transport, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Cerebratulus lacteus (milky ribbon-worm)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12350.54

構造登録者

Pesce, A.,Nardini, M.,Dewilde, S.,Geuens, E.,Yamauchi, k.,Ascenzi, P.,Riggs, A.F.,Moens, L.,Bolognesi, M. (登録日: 2002-01-09, 公開日: 2002-05-15, 最終更新日: 2024-02-14)

主引用文献

Pesce, A.,Nardini, M.,Dewilde, S.,Geuens, E.,Yamauchi, k.,Ascenzi, P.,Riggs, A.F.,Moens, L.,Bolognesi, M.
The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold
Structure, 10:725-735, 2002

PubMed Abstract: A very short hemoglobin (CerHb; 109 amino acids) binds O(2) cooperatively in the nerve tissue of the nemertean worm Cerebratulus lacteus to sustain neural activity during anoxia. Sequence analysis suggests that CerHb tertiary structure may be unique among the known globin fold evolutionary variants. The X-ray structure of oxygenated CerHb (R factor 15.3%, at 1.5 A resolution) displays deletion of the globin N-terminal A helix, an extended GH region, a very short H helix, and heme solvent shielding based on specific aromatic residues. The heme-bound O(2) is stabilized by hydrogen bonds to the distal TyrB10-GlnE7 pair. Ligand access to heme may take place through a wide protein matrix tunnel connecting the distal site to a surface cleft located between the E and H helices.

PubMed: 12015154
DOI: 10.1016/S0969-2126(02)00763-3

実験手法

X-RAY DIFFRACTION (1.5 Å)