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	The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 122, Issue 6, Page e2419884122, Year 2025
掲載日	2025年2月11日
著者	Heidi L Schubert / Feng Li / Christopher P Hill / Eric W Schmidt /
PubMed 要旨	The polyketide synthases (PKSs) in microbes and the cytoplasmic fatty acid synthases in humans (FASs) are related enzymes that have been well studied. As a result, there is a paradigm explaining in ...The polyketide synthases (PKSs) in microbes and the cytoplasmic fatty acid synthases in humans (FASs) are related enzymes that have been well studied. As a result, there is a paradigm explaining in general terms how FASs repeatedly use a set of enzymatic domains to produce simple fats, while PKSs use the domains in a much more complex manner to produce pharmaceuticals and other elaborate molecules. However, most animals also have PKSs that do not conform to the rules described in microbes, including a large family of enzymes that bridge fatty acid and polyketide metabolism, the animal FAS-like PKSs (AFPKs). Here, we present the cryoelectron microscopy structures of two AFPKs from sea slugs. While the AFPK resemble mammalian FASs, their chemical products mimic those of PKSs in complexity. How then does the architecture of AFPKs facilitate this structural complexity? Unexpectedly, chemical complexity is controlled not solely by the enzymatic domains but is aided by the dynamics of the acyl carrier protein (ACP), a shuttle that moves intermediates between these domains. We observed interactions between enzyme domains and the linker-ACP domain, which, when manipulated, altered the kinetic properties of the enzyme to change the resulting chemical products. This unveils elaborate mechanisms and enzyme motions underlying lipid and polyketide biochemistry across the domains of life.
リンク	Proc Natl Acad Sci U S A / PubMed:39913209 / PubMed Central
手法	EM (単粒子)
解像度	2.92 - 4.3 Å
構造データ	45806 9cq1 EMDB-45806, PDB-9cq1: Condensing region of EcPKS1 手法: EM (単粒子) / 解像度: 4.3 Å 45812 9cq9 EMDB-45812, PDB-9cq9: Modifying region of EcPKS1 手法: EM (単粒子) / 解像度: 3.5 Å 45907 9cti EMDB-45907, PDB-9cti: Condensing region of EcPKS2 - malonylCoA inhibited dataset 手法: EM (単粒子) / 解像度: 3.03 Å 45909 9ctk EMDB-45909, PDB-9ctk: Modifying region of EcPKS2 - malonylCoA inhibited dataset 手法: EM (単粒子) / 解像度: 2.92 Å 45910 9ctl EMDB-45910, PDB-9ctl: Full length EcPKS2 - malonylCoA inhibited dataset 手法: EM (単粒子) / 解像度: 3.15 Å 45911 9ctm EMDB-45911, PDB-9ctm: Condensing region of EcPKS2 - acetylated dataset 手法: EM (単粒子) / 解像度: 2.92 Å 45912 9ctn EMDB-45912, PDB-9ctn: Modifying region of EcPKS2 - acetylated dataset 手法: EM (単粒子) / 解像度: 3.11 Å 45913 9cto EMDB-45913, PDB-9cto: Full length EcPKS2 - acylated dataset with three ACP positions 手法: EM (単粒子) / 解像度: 3.1 Å
化合物	ChemComp-MLC: MALONYL-COENZYME A / マロニルCoA ChemComp-NAP: NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE ChemComp-HOH: WATER ChemComp-NDP: NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / NADPH ChemComp-6VG: ~{S}-[2-[3-[[(2~{R})-3,3-dimethyl-2-oxidanyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] ethanethioate / S-アセチルホスホパンテテイン
由来	elysia chlorotica (無脊椎動物)
キーワード	BIOSYNTHETIC PROTEIN / polyketide adenosyl transferase / beta-keto-synthase / dehydratase / keto-redctase / Acyl carrier protein / beta-keto-synthase dehydratase / keto-reductase / polyketide adenosyl transferase beta-keto-synthase dehydratase keto-reductase Acyl carrier protein / polyketide synthase acetyltransferase ketoreductase ketosynthase dehydrogenase