2DC3

Crystal structure of human cytoglobin at 1.68 angstroms resolution

2DC3 の概要

• エントリーDOI: 10.2210/pdb2dc3/pdb
• 分子名称: Cytoglobin, PROTOPORPHYRIN IX CONTAINING FE, ACETIC ACID, ... (4 entities in total)
• 機能のキーワード: cytoglobin, myoglobin, heme, oxygen transport, oxygen storage, riken structural genomics/proteomics initiative, rsgi, structural genomics, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): Q8WWM9
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44724.81

構造登録者

Makino, M.,Sugimoto, H.,Sawai, H.,Kawada, N.,Yoshizato, K.,Shiro, Y.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-12-21, 公開日: 2006-05-23, 最終更新日: 2024-11-13)

主引用文献

Makino, M.,Sugimoto, H.,Sawai, H.,Kawada, N.,Yoshizato, K.,Shiro, Y.
High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode.
Acta Crystallogr.,Sect.D, 62:671-677, 2006

PubMed Abstract: Cytoglobin (Cgb) is a recently discovered member of the vertebrate haem-containing globin family. The structure of a new crystal form of wild-type human Cgb (space group C2) was determined at a resolution of 1.68 Angstrom. The results show the presence of an additional helix in the N-terminal residues (4-20) prior to the A helix and an ordered loop structure in the C-terminal region (168-188), while these extended peptides were invisible owing to disorder in the previously reported structures using a P3(2)21 crystal at a resolution of 2.4 Angstrom. A detailed comparison of the two crystal structures shows differences in the conformation of the residues (i.e. Arg84) in the haem environment owing to a different dimeric arrangement.

PubMed: 16699195
DOI: 10.1107/S0907444906013813

実験手法

X-RAY DIFFRACTION (1.68 Å)