1L2K

Neutron Structure Determination of Sperm Whale Met-Myoglobin at 1.5A Resolution.

1L2K の概要

• エントリーDOI: 10.2210/pdb1l2k/pdb
• 分子名称: MYOGLOBIN, SULFATE ION, AMMONIUM CATION WITH D, ... (5 entities in total)
• 機能のキーワード: neutron structure, hydrogen atoms, hydration structure, heme protein, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Physeter catodon (sperm whale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18065.63

構造登録者

Ostermann, A.,Tanaka, I.,Engler, N.,Niimura, N.,Parak, F.G. (登録日: 2002-02-21, 公開日: 2002-08-21, 最終更新日: 2024-04-03)

主引用文献

Ostermann, A.,Tanaka, I.,Engler, N.,Niimura, N.,Parak, F.G.
Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 A resolution.
Biophys.Chem., 95:183-193, 2002

PubMed Abstract: From the first days of protein neutron structure determination sperm whale myoglobin was an object under investigation [Nature 224 (1969) 143, J. Mol. Biol. 220 (1991) 381]. Nevertheless myoglobin is still of interest [Proc. Natl. Acad. Sci. USA 97 (2000) 3872]. The feasibility of the monochromatic neutron diffractometer BIX-3 at the JRR-3M reactor at the JAERI [J. Phys. Chem. Solids 60 (1999) 1623], to collect high-resolution diffraction data in a relatively short time stimulated us to repeat the structural determination of myoglobin. The structure of metmyoglobin has been determined up to a resolution of 1.5 A. The hydrogen atoms were replaced in part, by deuterium soaking the crystals for more than 10 years in D(2)O. A refinement of all atoms has been performed including the refinement of individual mean square displacements and occupancies of the exchangeable protons in backbone hydrogen bonds. A method is described to show clear negative scattering densities of the H atoms. Water molecules within the protein and on the molecule surface are shown. The exchangeability of H atoms is correlated with structural distribution and flexibility.

PubMed: 12062378
DOI: 10.1016/S0301-4622(01)00255-1

実験手法

NEUTRON DIFFRACTION (1.5 Å)