- EMDB-1505: Structural basis for the regulated protease and chaperone functio... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-1505
タイトル
Structural basis for the regulated protease and chaperone function of DegP
マップデータ
Cryo EM structure of the DegP12-OMP complex
試料
試料: DegP dodecamer with bound OMP
タンパク質・ペプチド: DegP
キーワード
protease-chaperone / electron microscopy / single particle analysis
機能・相同性
機能・相同性情報
peptidase Do / response to temperature stimulus / porin activity / pore complex / protein quality control for misfolded or incompletely synthesized proteins / chaperone-mediated protein folding / monoatomic ion transmembrane transport / serine-type peptidase activity / cell outer membrane / protein folding ...peptidase Do / response to temperature stimulus / porin activity / pore complex / protein quality control for misfolded or incompletely synthesized proteins / chaperone-mediated protein folding / monoatomic ion transmembrane transport / serine-type peptidase activity / cell outer membrane / protein folding / virus receptor activity / peptidase activity / outer membrane-bounded periplasmic space / response to heat / response to oxidative stress / receptor-mediated virion attachment to host cell / serine-type endopeptidase activity / DNA damage response / proteolysis / identical protein binding / metal ion binding / plasma membrane 類似検索 - 分子機能
Peptidase S1C, Do / Porin, gammaproteobacterial / Porin, Gram-negative type, conserved site / General diffusion Gram-negative porins signature. / Gram-negative porin / Porin, Gram-negative type / Peptidase S1C / Trypsin-like peptidase domain / Porin domain superfamily / PDZ domain ...Peptidase S1C, Do / Porin, gammaproteobacterial / Porin, Gram-negative type, conserved site / General diffusion Gram-negative porins signature. / Gram-negative porin / Porin, Gram-negative type / Peptidase S1C / Trypsin-like peptidase domain / Porin domain superfamily / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Peptidase S1, PA clan 類似検索 - ドメイン・相同性
Outer membrane porin C / Periplasmic serine endoprotease DegP 類似検索 - 構成要素
ジャーナル: Nature / 年: 2008 タイトル: Structural basis for the regulated protease and chaperone function of DegP. 著者: Tobias Krojer / Justyna Sawa / Eva Schäfer / Helen R Saibil / Michael Ehrmann / Tim Clausen / 要旨: All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock protein DegP is a protein quality control factor in the bacterial envelope that is involved in ...All organisms have to monitor the folding state of cellular proteins precisely. The heat-shock protein DegP is a protein quality control factor in the bacterial envelope that is involved in eliminating misfolded proteins and in the biogenesis of outer-membrane proteins. Here we describe the molecular mechanisms underlying the regulated protease and chaperone function of DegP from Escherichia coli. We show that binding of misfolded proteins transforms hexameric DegP into large, catalytically active 12-meric and 24-meric multimers. A structural analysis of these particles revealed that DegP represents a protein packaging device whose central compartment is adaptable to the size and concentration of substrate. Moreover, the inner cavity serves antagonistic functions. Whereas the encapsulation of folded protomers of outer-membrane proteins is protective and might allow safe transit through the periplasm, misfolded proteins are eliminated in the molecular reaction chamber. Oligomer reassembly and concomitant activation on substrate binding may also be critical in regulating other HtrA proteases implicated in protein-folding diseases.
想定した対称性 - 点群: C1 (非対称) / アルゴリズム: OTHER / 解像度のタイプ: BY AUTHOR / 解像度: 28.0 Å / 解像度の算出法: FSC 0.5 CUT-OFF / ソフトウェア - 名称: SPIDER and IMAGIC / 詳細: no symmetry was use for the calculation of the map / 使用した粒子像数: 6285