超膜二酸化リン結合タンパク質複合体のデノボデザインと分子組成
Ivan V Korendovych1, Alessandro Senes, Yong Ho Kim
1Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Journal of the American Chemical Society
|October 16, 2010
まとめ
研究者らは,精密に配置されたポルフィリンを使用して,トランスメブラン電子転送を促進するために,新しい膜タンパク質"PRIME"を設計した. この画期的な発見は,潜在的バイオエレクトロニクスアプリケーションのための膜タンパク質の新しい設計を進めている.
科学分野:
- バイオケミストリー バイオケミストリー
- 構造生物学 構造生物学とは
- バイオ・オーガニック化学 バイオ・オーガニック化学
背景:
- 膜タンパク質のデノボ設計は,大変な課題です.
- タンパク質の折りたたみと結合を理解することは鍵です.
- 膜間電子伝達は,特定のタンパク質構造を必要とします.
研究 の 目的:
- PRIME (Porphyrins In Membrane) という新しい膜タンパク質を設計する.
- 精密に配置されたポルフィリン経由でトランスメブラン電子伝送を可能にするために.
- 計算設計法を膜タンパク質標的に拡張する.
主な方法:
- 計算によるタンパク質設計.
- D (((2) -対称な螺旋束の配列.
- 顕微鏡および生体物理的特徴付け (UV-vis,CD,AUC,リドックス電位計,EPR) について.
主要な成果:
- PRIME膜タンパク質の設計と合成に成功しました.
- PRIMEは2つの鉄二フェニルポルフィリンを電子移転のために配置します.
- bis-His幾何学におけるコファクター結合に対する高い親和性と特異性を実証した.
- 二次殻の水素結合は,ポルフィリン結合部位を安定させる.
結論:
- PRIMEは,電子移転のための膜タンパク質の新しい設計を成功させました.
- この研究では,複雑な膜タンパク質構造を設計するための計算方法が検証されています.
- この研究は,バイオエレクトロニクスとエネルギー変換におけるエンジニアリングされた膜タンパク質への道を開きます.
関連する概念動画
Structure of Porins
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...
Multi-pass Transmembrane Proteins and β-barrels
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Porin Insertion in the Outer Mitochondrial Membrane
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Insertion of Multi-pass Transmembrane Proteins in the RER
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Insertion of Single-pass Transmembrane Proteins in the RER
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...


