1TU5

Crystal structure of bovine plasma copper-containing amine oxidase

1TU5 の概要

• エントリーDOI: 10.2210/pdb1tu5/pdb
• 関連するPDBエントリー: 1KSI 1N9E 1OAC
• 関連するBIRD辞書のPRD_ID: PRD_900017
• 分子名称: Copper amine oxidase, liver isozyme, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: amine oxidase, oxidoreductase, quinoenzyme, tpq
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Secreted, extracellular space: Q29437
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 168216.18

構造登録者

Lunelli, M.,Di Paolo, M.L.,Biadene, M.,Calderone, V.,Scarpa, M.,Battistutta, R.,Rigo, A.,Zanotti, G. (登録日: 2004-06-24, 公開日: 2005-02-22, 最終更新日: 2023-10-25)

主引用文献

Lunelli, M.,Di Paolo, M.L.,Biadene, M.,Calderone, V.,Battistutta, R.,Scarpa, M.,Rigo, A.,Zanotti, G.
Crystal structure of amine oxidase from bovine serum.
J.Mol.Biol., 346:991-1004, 2005

PubMed Abstract: Copper-containing amine oxidase extracted from bovine serum (BSAO) was crystallized and its three-dimensional structure at 2.37A resolution is described. The biological unit of BSAO is a homodimer, formed by two monomers related to each other by a non-crystallographic 2-fold axis. Each monomer is composed of three domains, similar to those of other amine oxidases from lower species. The two monomers are structurally equivalent, despite some minor differences at the two active sites. A large funnel allows access of substrates to the active-site; another cavity, accessible to the solvent, is also present between the two monomers; this second cavity could allow the entrance of molecular oxygen necessary for the oxidative reaction. Some sugar residues, bound to Asn, were still present and visible in the electron density map, in spite of the exhaustive deglycosylation necessary to grow the crystals. The comparison of the BSAO structure with those of other resolved AO structures shows strong dissimilarities in the architecture and charge distribution of the cavities leading to the active-site, possibly explaining the differences in substrate specificity.

PubMed: 15701511
DOI: 10.1016/j.jmb.2004.12.038

実験手法

X-RAY DIFFRACTION (2.37 Å)