EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structures of methane and ammonia monooxygenases in native membranes.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 122, Issue 1, Page e2417993121, Year 2025
掲載日	2025年1月7日
著者	Frank J Tucci / Amy C Rosenzweig /
PubMed 要旨	Methane- and ammonia-oxidizing bacteria play key roles in the global carbon and nitrogen cycles, respectively. These bacteria use homologous copper membrane monooxygenases to accomplish the defining ...Methane- and ammonia-oxidizing bacteria play key roles in the global carbon and nitrogen cycles, respectively. These bacteria use homologous copper membrane monooxygenases to accomplish the defining chemical transformations of their metabolisms: the oxidations of methane to methanol by particulate methane monooxygenase (pMMO) and ammonia to hydroxylamine by ammonia monooxygenase (AMO), enzymes of prime interest for applications in mitigating climate change. However, investigations of these enzymes have been hindered by the need for disruptive detergent solubilization prior to structure determination, confounding studies of pMMO and precluding studies of AMO. Here, we overcome these challenges by using cryoEM to visualize pMMO and AMO directly in their native membrane arrays at 2.4 to 2.8 Å resolution. These structures reveal details of the copper centers, numerous bound lipids, and previously unobserved components, including identifiable and distinct supernumerary helices interacting with pMMO and AMO, suggesting a widespread role for these helices in copper membrane monooxygenases. Comparisons between these structures, their metallocofactors, and their unexpected protein-protein interactions highlight features that may govern activity or the formation of higher-order arrays in native membranes. The ability to obtain molecular insights within the native membrane will enable further understanding of these environmentally important enzymes.
リンク	Proc Natl Acad Sci U S A / PubMed:39739801 / PubMed Central
手法	EM (単粒子)
解像度	2.42 - 2.89 Å
構造データ	45658 9cl1 EMDB-45658, PDB-9cl1: Particulate methane monooxygenase in 0.02% DDM 手法: EM (単粒子) / 解像度: 2.89 Å 45659 9cl2 EMDB-45659, PDB-9cl2: Particulate methane monooxygenase in washed native membranes 手法: EM (単粒子) / 解像度: 2.42 Å 45660 9cl3 EMDB-45660, PDB-9cl3: Particulate methane monooxygenase in unwashed native membranes 手法: EM (単粒子) / 解像度: 2.59 Å 45661 9cl4 EMDB-45661, PDB-9cl4: Particulate methane monooxygenase in crosslinked, washed native membranes 手法: EM (単粒子) / 解像度: 2.61 Å 45662 9cl5 EMDB-45662, PDB-9cl5: particulate methane monooxygenase in native membranes 手法: EM (単粒子) / 解像度: 2.48 Å 45663 9cl6 EMDB-45663, PDB-9cl6: Ammonia monooxygenase in native membranes 手法: EM (単粒子) / 解像度: 2.77 Å
化合物	ChemComp-CU: COPPER (II) ION ChemComp-HOH: WATER PDB-1a0p: SITE-SPECIFIC RECOMBINASE, XERD
由来	methylococcus capsulatus str. bath (バクテリア) methylocystis sp. atcc 49242 (バクテリア) nitrosomonas europaea atcc 19718 (バクテリア)
キーワード	OXIDOREDUCTASE / membrane protein / metalloenzyme / monooxygenase