1CJE

ADRENODOXIN FROM BOVINE

1CJE の概要

• エントリーDOI: 10.2210/pdb1cje/pdb
• NMR情報: BMRB: 5337
• 分子名称: ADRENODOXIN, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• 機能のキーワード: electron transport protein, iron sulfur protein, 2fe-2s ferredoxin, electron transport
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56602.01

構造登録者

Pikuleva, I.A.,Tesh, K.,Waterman, M.R.,Kim, Y. (登録日: 1999-04-12, 公開日: 2000-01-21, 最終更新日: 2023-08-09)

主引用文献

Pikuleva, I.A.,Tesh, K.,Waterman, M.R.,Kim, Y.
The tertiary structure of full-length bovine adrenodoxin suggests functional dimers.
Arch.Biochem.Biophys., 373:44-55, 2000

PubMed Abstract: The three-dimensional X-ray crystal structure of full-length oxidized bovine adrenodoxin (Adx) has been determined at 2.5 A resolution by molecular replacement using a structure of a truncated form as a starting model. Crystals of Adx belong to a primitive monoclinic space group P2(1) with four Adx molecules in an asymmetric unit. The unit cell dimensions are a = 59.44 A, b = 77.03 A, c = 59.68 A, and beta = 94.83 degrees. The structure has been refined to an R factor of 23.5%. Structures of the four molecules of full-length Adx (127 amino acids) in the asymmetric unit were compared with each other and also with that of the truncated Adx (4-108). The overall topology of full-length Adx remains the same as described earlier for the truncated protein. Differences that do occur are almost wholly confined to alternate side-chain conformations that reflect differing lattice contacts made by two proteins. Extensive interactions found between molecules 1 and 2 in the full-length Adx asymmetric unit may reflect the ability of Adx to form dimers in vivo and are consistent with hydrodynamic measurements which show that in solution there is an equilibrium between monomeric and dimeric forms of Adx. Dimerization of Adx could explain why the truncated form has greater affinity for the P450 redox partner than the full-length form. From these results it can be considered that the mechanism of electron transfer is not necessarily the same in different mitochondrial P450 systems.

PubMed: 10620322
DOI: 10.1006/abbi.1999.1536

実験手法

X-RAY DIFFRACTION (2.5 Å)