1X3X

Crystal Structure of Cytochrome b5 from Ascaris suum

1X3X の概要

• エントリーDOI: 10.2210/pdb1x3x/pdb
• 分子名称: Cytochrome b5, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: cytochrome b5, hemoprotein, porcine parasitic namatode, electron transport
• 由来する生物種: Ascaris suum (pig roundworm)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19648.30

構造登録者

Yokota, T.,Nakajima, Y.,Yamakura, F.,Sugio, S.,Hashimoto, M.,Takamiya, S.,Aoki, T. (登録日: 2005-05-11, 公開日: 2006-06-06, 最終更新日: 2024-10-30)

主引用文献

Yokota, T.,Nakajima, Y.,Yamakura, F.,Sugio, S.,Hashimoto, M.,Takamiya, S.
Unique structure of Ascaris suum b5-type cytochrome: an additional alpha-helix and positively charged residues on the surface domain interact with redox partners
Biochem.J., 394:437-447, 2006

PubMed Abstract: Cytochrome b5 of the body wall of adult Ascaris suum, a porcine parasitic nematode, is a soluble protein that lacks a C-terminal membrane-anchoring domain, but possesses an N-terminal pre-sequence of 30 amino acids. During the maturation of cytochrome b5, the N-terminal pre-sequence is proteolytically cleaved to form the mature protein of 82 amino acid residues. A. suum cytochrome b5 is a basic protein containing more lysine residues and exhibiting a higher midpoint redox potential than its mammalian counterparts. We developed an expression system for the production of the recombinant nematode cytochrome b5, which is chemically and functionally identical with the native protein. Using this recombinant protein, we have determined the X-ray crystal structure of A. suum cytochrome b5 at 1.8 A (1 A=0.1 nm) resolution, and we have shown that this protein is involved in the reduction of nematode body-wall metmyoglobin. The crystal structure of A. suum cytochrome b5 consists of six alpha-helices and five beta-strands. It differs from its mammalian counterparts by having a head-to-tail disulphide bridge, as well as a four-residue insertion in the vicinity of the sixth ligating histidine, which forms an additional alpha-helix, alpha4A, between helices alpha4 and alpha5. A. suum cytochrome b5 exists predominantly as a haem-orientation B isomer. Furthermore, the haem plane is rotated approx. 80 degrees relative to the axis formed by haem-Fe and N atoms of the two histidine residues that are ligated to haem-Fe. The charge distribution around the haem crevice of A. suum cytochrome b5 is remarkably different from that of mammalian cytochrome b5 in that the nematode protein bears positively charged lysine residues surrounding the haem crevice. Using immunohistochemistry, we found that A. suum cytochrome b5 is present in the nematode hypodermis. Based on this histochemical and structural information, the physiological function of A. suum cytochrome b5 and its interaction with nematode metmyoglobin can be hypothesized.

PubMed: 16288599
DOI: 10.1042/BJ20051308

実験手法

X-RAY DIFFRACTION (1.8 Å)