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	IMPDH1 retinal variants control filament architecture to tune allosteric regulation.
ジャーナル・号・ページ	Nat Struct Mol Biol, Vol. 29, Issue 1, Page 47-58, Year 2022
掲載日	2022年1月10日
著者	Anika L Burrell / Chuankai Nie / Meerit Said / Jacqueline C Simonet / David Fernández-Justel / Matthew C Johnson / Joel Quispe / Rubén M Buey / Jeffrey R Peterson / Justin M Kollman /
PubMed 要旨	Inosine-5'-monophosphate dehydrogenase (IMPDH), a key regulatory enzyme in purine nucleotide biosynthesis, dynamically assembles filaments in response to changes in metabolic demand. Humans have two ...Inosine-5'-monophosphate dehydrogenase (IMPDH), a key regulatory enzyme in purine nucleotide biosynthesis, dynamically assembles filaments in response to changes in metabolic demand. Humans have two isoforms: IMPDH2 filaments reduce sensitivity to feedback inhibition, while IMPDH1 assembly remains uncharacterized. IMPDH1 plays a unique role in retinal metabolism, and point mutants cause blindness. Here, in a series of cryogenic-electron microscopy structures we show that human IMPDH1 assembles polymorphic filaments with different assembly interfaces in extended and compressed states. Retina-specific splice variants introduce structural elements that reduce sensitivity to GTP inhibition, including stabilization of the extended filament form. Finally, we show that IMPDH1 disease mutations fall into two classes: one disrupts GTP regulation and the other has no effect on GTP regulation or filament assembly. These findings provide a foundation for understanding the role of IMPDH1 in retinal function and disease and demonstrate the diverse mechanisms by which metabolic enzyme filaments are allosterically regulated.
リンク	Nat Struct Mol Biol / PubMed:35013599 / PubMed Central
手法	EM (単粒子)
解像度	2.4 - 3.9 Å
構造データ	24437 7rer EMDB-24437, PDB-7rer: HUMAN IMPDH1 TREATED WITH ATP, IMP, AND NAD+ 手法: EM (単粒子) / 解像度: 2.6 Å 24438 7res EMDB-24438: HUMAN IMPDH1 TREATED WITH ATP, IMP, AND NAD+; OCTAMER-CENTERED PDB-7res: HUMAN IMPDH1 TREATED WITH ATP, IMP, AND NAD+, OCTAMER-CENTERED 手法: EM (単粒子) / 解像度: 3.05 Å 24439 7rfe EMDB-24439, PDB-7rfe: HUMAN IMPDH1 TREATED WITH GTP, IMP, AND NAD+; INTERFACE-CENTERED 手法: EM (単粒子) / 解像度: 2.6 Å 24440 7rff EMDB-24440, PDB-7rff: HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH ATP; INTERFACE-CENTERED 手法: EM (単粒子) / 解像度: 2.7 Å 24441 7rfg EMDB-24441, PDB-7rfg: HUMAN IMPDH1 TREATED WITH GTP, IMP, AND NAD+ OCTAMER-CENTERED 手法: EM (単粒子) / 解像度: 2.6 Å 24442 7rfh EMDB-24442, PDB-7rfh: HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH ATP, OCTAMER-CENTERED 手法: EM (単粒子) / 解像度: 3.7 Å 24443 7rfi EMDB-24443, PDB-7rfi: HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH GTP, ATP, IMP, NAD+, INTERFACE-CENTERED 手法: EM (単粒子) / 解像度: 2.6 Å 24448 7rgd EMDB-24448, PDB-7rgd: HUMAN RETINAL VARIANT IMPDH1(595) TREATED WITH GTP, ATP, IMP, NAD+, OCTAMER-CENTERED 手法: EM (単粒子) / 解像度: 3.0 Å 24450 7rgi EMDB-24450, PDB-7rgi: HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH GTP, ATP, IMP, NAD+; INTERFACE-CENTERED 手法: EM (単粒子) / 解像度: 3.6 Å 24451 7rgl EMDB-24451, PDB-7rgl: HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH ATP, IMP, NAD+, INTERFACE-CENTERED 手法: EM (単粒子) / 解像度: 2.4 Å 24452 7rgm EMDB-24452, PDB-7rgm: HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH ATP, IMP, NAD+, OCTAMER-CENTERED 手法: EM (単粒子) / 解像度: 2.8 Å 24454 7rgq EMDB-24454, PDB-7rgq: HUMAN RETINAL VARIANT IMPDH1(546) TREATED WITH GTP, ATP, IMP, NAD+; INTERFACE-CENTERED 手法: EM (単粒子) / 解像度: 3.9 Å
化合物	ChemComp-NAD: NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NADYM / ニコチンアミドアデニンジヌクレオチド ChemComp-IMP: INOSINIC ACID / IMP / イノシン酸 ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM / アデノシン三リン酸 ChemComp-GTP: GUANOSINE-5'-TRIPHOSPHATE / GTP / GTP, エネルギー貯蔵分子*YM / グアノシン三リン酸
由来	homo sapiens (ヒト)
キーワード	OXIDOREDUCTASE (酸化還元酵素) / METABOLISM (代謝) / FILAMENT / ALLOSTERY (アロステリック効果) / ADENINE (アデニン)