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	Structure and catalytic mechanism of exogenous fatty acid recycling by AasS, a versatile acyl-ACP synthetase.
ジャーナル・号・ページ	Nat Struct Mol Biol, Vol. 32, Issue 5, Page 802-817, Year 2025
掲載日	2025年1月10日
著者	Haomin Huang / Chen Wang / Shenghai Chang / Tao Cui / Yongchang Xu / Man Huang / Huimin Zhang / Chun Zhou / Xing Zhang / Youjun Feng /
PubMed 要旨	Fatty acids (FAs) are essential building blocks for all the domains of life, of which bacterial de novo synthesis, called type II FA synthesis (FAS II), is energetically expensive. The recycling of ...Fatty acids (FAs) are essential building blocks for all the domains of life, of which bacterial de novo synthesis, called type II FA synthesis (FAS II), is energetically expensive. The recycling of exogenous FAs (eFAs) partially relieves the FAS II demand and, therefore, compromises the efficacy of FAS II-directed antimicrobials. The versatile acyl-acyl carrier protein (ACP) synthetase, AasS, enables bacterial channeling of diverse eFA nutrients through holo-ACP, an activated form of ACP. However, the molecular mechanism for AasS catalysis is not fully understood. Here we report a series of cryo-electron microscopy structures of AasS from the bioluminescent bacterium Vibrio harveyi to provide insights into the catalytic cycle. AasS forms a ring-shaped hexamer, with each protomer folding into two distinct domains. Biochemical and structural analysis suggests that AasS accommodates distinct eFA substrates and the conserved W230 residue has a gating role. Adenosine triphosphate and Mg binding converts the AasS hexamer to a tetramer, which is likely needed for the acyl adenylate intermediate formation. Afterward, AasS reverts to the hexamer conformation in adaption to acyl-ACP production. The complete landscape for eFA scavenging lays a foundation for exploiting the versatility of AasS in biopharmaceuticals.
リンク	Nat Struct Mol Biol / PubMed:39794554 / PubMed Central
手法	EM (単粒子)
解像度	2.41 - 2.76 Å
構造データ	35144 8i35 EMDB-35144, PDB-8i35: Acyl-ACP synthetase structure bound to oleic acid 手法: EM (単粒子) / 解像度: 2.75 Å 35153 8i3i EMDB-35153, PDB-8i3i: Acyl-ACP synthetase structure bound to AMP-PNP in the presence of MgCl2 手法: EM (単粒子) / 解像度: 2.68 Å 35165 8i49 EMDB-35165: Acyl-ACP synthetase structure bound to ATP. PDB-8i49: Acyl-ACP synthetase structure bound to ATP 手法: EM (単粒子) / 解像度: 2.41 Å 35190 8i51 EMDB-35190, PDB-8i51: Acyl-ACP synthetase structure bound to AMP-MC7 手法: EM (単粒子) / 解像度: 2.76 Å 35200 8i6m EMDB-35200, PDB-8i6m: Acyl-ACP synthetase structure bound to AMP-C18:1 手法: EM (単粒子) / 解像度: 2.59 Å 35248 8i8d EMDB-35248, PDB-8i8d: Acyl-ACP synthetase structure bound to MC7-ACP 手法: EM (単粒子) / 解像度: 2.51 Å 35249 8i8e EMDB-35249, PDB-8i8e: Acyl-ACP synthetase structure bound to C18:1-ACP 手法: EM (単粒子) / 解像度: 2.63 Å
化合物	ChemComp-OLA: OLEIC ACID ChemComp-MG: Unknown entry ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, エネルギー貯蔵分子類似体YM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, エネルギー貯蔵分子YM ChemComp-AMP: ADENOSINE MONOPHOSPHATE / AMPYM ChemComp-OP3: 7-methoxy-7-oxidanylidene-heptanoic acid ChemComp-PN7*: N~3~-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-N-(2-sulfanylethyl)-beta-alaninamide
由来	vibrio harveyi (バクテリア) escherichia coli (大腸菌)
キーワード	CYTOSOLIC PROTEIN / Acyl-ACP synthetase / Tool enzyme / TRANSFERASE / CYTOSOLIC PROTEIN/TRANSPORT PROTEIN / Ligase / CYTOSOLIC PROTEIN-TRANSPORT PROTEIN complex / TRANSPORT PROTEIN/CYTOSOLIC PROTEIN / TRANSPORT PROTEIN-CYTOSOLIC PROTEIN complex