6AY0

Crystal structure of H108A peptidylglycine alpha-hydroxylating monooxygenase (PHM) soaked with peptide

6AY0 の概要

• エントリーDOI: 10.2210/pdb6ay0/pdb
• 分子名称: Peptidyl-glycine alpha-amidating monooxygenase, COPPER (II) ION (3 entities in total)
• 機能のキーワード: peptidylglycine monooxygenase, peptidylglycine 2-hydroxylase, phm, oxidoreductase
• 由来する生物種: Rattus norvegicus (Rat)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34770.36

構造登録者

Maheshwari, S.,Rudzka, K.,Gabelli, S.B.,Amzel, L.M. (登録日: 2017-09-07, 公開日: 2018-07-18, 最終更新日: 2024-11-13)

主引用文献

Maheshwari, S.,Shimokawa, C.,Rudzka, K.,Kline, C.D.,Eipper, B.A.,Mains, R.E.,Gabelli, S.B.,Blackburn, N.,Amzel, L.M.
Effects of copper occupancy on the conformational landscape of peptidylglycine alpha-hydroxylating monooxygenase.
Commun Biol, 1:74-74, 2018

PubMed Abstract: The structures of metalloproteins that use redox-active metals for catalysis are usually exquisitely folded in a way that they are prearranged to accept their metal cofactors. Peptidylglycine α-hydroxylating monooxygenase (PHM) is a dicopper enzyme that catalyzes hydroxylation of the α-carbon of glycine-extended peptides for the formation of des-glycine amidated peptides. Here, we present the structures of apo-PHM and of mutants of one of the copper sites (H107A, H108A, and H172A) determined in the presence and absence of citrate. Together, these structures show that the absence of one copper changes the conformational landscape of PHM. In one of these structures, a large interdomain rearrangement brings residues from both copper sites to coordinate a single copper (closed conformation) indicating that full copper occupancy is necessary for locking the catalytically competent conformation (open). These data suggest that in addition to their required participation in catalysis, the redox-active metals play an important structural role.

PubMed: 30271955
DOI: 10.1038/s42003-018-0082-y

実験手法

X-RAY DIFFRACTION (2.6 Å)