5HMA

Crystal structure of MamO protease domain from Magnetospirillum magneticum (Ni bound form)

5HMA の概要

• エントリーDOI: 10.2210/pdb5hma/pdb
• 関連するPDBエントリー: 5HM9
• 分子名称: Trypsin-like serine protease, Unidentified peptide, NICKEL (II) ION, ... (5 entities in total)
• 機能のキーワード: trypsin, biomineralization, pseudo-protease, magnetosome, hydrolase
• 由来する生物種: Magnetospirillum magneticum (strain AMB-1 / ATCC 700264); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 20230.23

構造登録者

Hershey, D.M.,Ren, X.,Hurley, J.H.,Komeili, A. (登録日: 2016-01-15, 公開日: 2016-02-10, 最終更新日: 2024-11-20)

主引用文献

Hershey, D.M.,Ren, X.,Melnyk, R.A.,Browne, P.J.,Ozyamak, E.,Jones, S.R.,Chang, M.C.,Hurley, J.H.,Komeili, A.
MamO Is a Repurposed Serine Protease that Promotes Magnetite Biomineralization through Direct Transition Metal Binding in Magnetotactic Bacteria.
Plos Biol., 14:e1002402-e1002402, 2016

PubMed Abstract: Many living organisms transform inorganic atoms into highly ordered crystalline materials. An elegant example of such biomineralization processes is the production of nano-scale magnetic crystals in magnetotactic bacteria. Previous studies implicated the involvement of two putative serine proteases, MamE and MamO, during the early stages of magnetite formation in Magnetospirillum magneticum AMB-1. Here, using genetic analysis and X-ray crystallography, we show that MamO has a degenerate active site, rendering it incapable of protease activity. Instead, MamO promotes magnetosome formation through two genetically distinct, noncatalytic activities: activation of MamE-dependent proteolysis of biomineralization factors and direct binding to transition metal ions. By solving the structure of the protease domain bound to a metal ion, we identify a surface-exposed di-histidine motif in MamO that contributes to metal binding and show that it is required to initiate biomineralization in vivo. Finally, we find that pseudoproteases are widespread in magnetotactic bacteria and that they have evolved independently in three separate taxa. Our results highlight the versatility of protein scaffolds in accommodating new biochemical activities and provide unprecedented insight into the earliest stages of biomineralization.

PubMed: 26981620
DOI: 10.1371/journal.pbio.1002402

実験手法

X-RAY DIFFRACTION (2.299 Å)