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	4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 107, Issue 11, Page 4967-4972, Year 2010
掲載日	2010年3月16日
著者	Yao Cong / Matthew L Baker / Joanita Jakana / David Woolford / Erik J Miller / Stefanie Reissmann / Ramya N Kumar / Alyssa M Redding-Johanson / Tanveer S Batth / Aindrila Mukhopadhyay / Steven J Ludtke / Judith Frydman / Wah Chiu /
PubMed 要旨	The essential double-ring eukaryotic chaperonin TRiC/CCT (TCP1-ring complex or chaperonin containing TCP1) assists the folding of approximately 5-10% of the cellular proteome. Many TRiC substrates ...The essential double-ring eukaryotic chaperonin TRiC/CCT (TCP1-ring complex or chaperonin containing TCP1) assists the folding of approximately 5-10% of the cellular proteome. Many TRiC substrates cannot be folded by other chaperonins from prokaryotes or archaea. These unique folding properties are likely linked to TRiC's unique heterooligomeric subunit organization, whereby each ring consists of eight different paralogous subunits in an arrangement that remains uncertain. Using single particle cryo-EM without imposing symmetry, we determined the mammalian TRiC structure at 4.7-A resolution. This revealed the existence of a 2-fold axis between its two rings resulting in two homotypic subunit interactions across the rings. A subsequent 2-fold symmetrized map yielded a 4.0-A resolution structure that evinces the densities of a large fraction of side chains, loops, and insertions. These features permitted unambiguous identification of all eight individual subunits, despite their sequence similarity. Independent biochemical near-neighbor analysis supports our cryo-EM derived TRiC subunit arrangement. We obtained a Calpha backbone model for each subunit from an initial homology model refined against the cryo-EM density. A subsequently optimized atomic model for a subunit showed approximately 95% of the main chain dihedral angles in the allowable regions of the Ramachandran plot. The determination of the TRiC subunit arrangement opens the way to understand its unique function and mechanism. In particular, an unevenly distributed positively charged wall lining the closed folding chamber of TRiC differs strikingly from that of prokaryotic and archaeal chaperonins. These interior surface chemical properties likely play an important role in TRiC's cellular substrate specificity.
リンク	Proc Natl Acad Sci U S A / PubMed:20194787 / PubMed Central
手法	EM (単粒子)
解像度	4.0 - 4.7 Å
構造データ	5145 3iyg 3ktt EMDB-5145: 4.7 Angstrom asymmetric cryo-EM map of TRiC in the both-ring closed ATP-AlFx state PDB-3iyg: Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map PDB-3ktt: Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map 手法: EM (単粒子) / 解像度: 4.7 Å 5148 3iyg 3ktt EMDB-5148: 4.0 Angstrom two-fold imposed cryo-EM map of TRiC in the both-ring closed ATP-AlFx state PDB-3iyg: Ca model of bovine TRiC/CCT derived from a 4.0 Angstrom cryo-EM map PDB-3ktt: Atomic model of bovine TRiC CCT2(beta) subunit derived from a 4.0 Angstrom cryo-EM map 手法: EM (単粒子) / 解像度: 4.0 Å
由来	bos taurus (ウシ)
キーワード	CHAPERONE (シャペロン) / TRiC/CCT / Asymmetric / Cryo-EM (低温電子顕微鏡法) / subunit arrangement / ATP-binding / Isopeptide bond / Nucleotide-binding / Phosphoprotein / Disulfide bond (ジスルフィド) / CCT2(beta) / Acetylation (アセチル化) / Cytoplasm (細胞質)