3PHM

REDUCED (CU+) PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE (PHM)

3PHM の概要

• エントリーDOI: 10.2210/pdb3phm/pdb
• 関連するPDBエントリー: 1OPM 1PHM
• 分子名称: PROTEIN (PEPTIDYLGLYCINE ALPHA-HYDROXYLATING MONOOXYGENASE), COPPER (II) ION, AZIDE ION, ... (6 entities in total)
• 機能のキーワード: monooxygenase, bioactive peptide activation, ascorbate, oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein: P14925
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35265.92

構造登録者

Prigge, S.T.,Amzel, L.M. (登録日: 1999-05-25, 公開日: 1999-09-29, 最終更新日: 2024-10-30)

主引用文献

Prigge, S.T.,Kolhekar, A.S.,Eipper, B.A.,Mains, R.E.,Amzel, L.M.
Substrate-mediated electron transfer in peptidylglycine alpha-hydroxylating monooxygenase.
Nat.Struct.Biol., 6:976-983, 1999

PubMed Abstract: Peptide amidation is a ubiquitous posttranslational modification of bioactive peptides. Peptidylglycine alpha-hydroxylating monooxygenase (PHM; EC 1.14.17.3), the enzyme that catalyzes the first step of this reaction, is composed of two domains, each of which binds one copper atom. The coppers are held 11 A apart on either side of a solvent-filled interdomain cleft, and the PHM reaction requires electron transfer between these sites. A plausible mechanism for electron transfer might involve interdomain motion to decrease the distance between the copper atoms. Our experiments show that PHM catalytic core (PHMcc) is enzymatically active in the crystal phase, where interdomain motion is not possible. Instead, structures of two states relevant to catalysis indicate that water, substrate and active site residues may provide an electron transfer pathway that exists only during the PHM catalytic cycle.

PubMed: 10504734
DOI: 10.1038/13351

実験手法

X-RAY DIFFRACTION (2.1 Å)