4E7V

The structure of R6 bovine insulin

4E7V の概要

• エントリーDOI: 10.2210/pdb4e7v/pdb
• 関連するPDBエントリー: 4E7T 4E7u
• 分子名称: Insulin A chain, Insulin B chain, M-CRESOL, ... (6 entities in total)
• 機能のキーワード: zinc binding, hormone
• 由来する生物種: Bos taurus (bovine,cow,domestic cattle,domestic cow); 詳細
• 細胞内の位置: Secreted: P01317 P01317
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 94434.26

構造登録者

Harris, P.,Frankaer, C.G.,Knudsen, M.V. (登録日: 2012-03-19, 公開日: 2012-04-04, 最終更新日: 2024-10-30)

主引用文献

Frankar, C.G.,Knudsen, M.V.,Noren, K.,Nazarenko, E.,Stahl, K.,Harris, P.
The structures of T(6), T(3)R(3) and R(6) bovine insulin: combining X-ray diffraction and absorption spectroscopy.
Acta Crystallogr.,Sect.D, 68:1259-1271, 2012

PubMed Abstract: The crystal structures of three conformations, T(6), T(3)R(3) and R(6), of bovine insulin were solved at 1.40, 1.30 and 1.80 Å resolution, respectively. All conformations crystallized in space group R3. In contrast to the T(6) and T(3)R(3) structures, different conformations of the N-terminal B-chain residue PheB1 were observed in the R(6) insulin structure, resulting in an eightfold doubling of the unit-cell volume upon cooling. The zinc coordination in each conformation was studied by X-ray absorption spectroscopy (XAS), including both EXAFS and XANES. Zinc adopts a tetrahedral coordination in all R(3) sites and an octahedral coordination in T(3) sites. The coordination distances were refined from XAS with a standard deviation of <0.01 Å. In contrast to the distances determined from the medium-resolution crystal structures, the XAS results were in good agreement with similar coordination geometries found in small molecules, as well as in other high-resolution insulin structures. As the radiation dose for XRD experiments is two orders of magnitude higher compared with that of XAS experiments, the single crystals were exposed to a higher degree of radiation damage that affected the zinc coordination in the T(3) sites in particular. Furthermore, XANES spectra for the zinc sites in T(6) and R(6) insulin were successfully calculated using finite difference methods and the bond distances and angles were optimized from a quantitative XANES analysis.

PubMed: 22993080
DOI: 10.1107/S090744491202625X

実験手法

X-RAY DIFFRACTION (1.8 Å)