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関連する概念動画

Molecular Models02:00

Molecular Models

Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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関連する実験動画

Updated: May 24, 2026

Visualizing Single Molecular Complexes In Vivo Using Advanced Fluorescence Microscopy
11:26

Visualizing Single Molecular Complexes In Vivo Using Advanced Fluorescence Microscopy

Published on: September 8, 2009

B12依存メチルトランスフェラーゼ複合体内の分子ジャグリングを視覚化.

Yan Kung1, Nozomi Ando, Tzanko I Doukov

  • 1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.

Nature
|March 16, 2012
PubMed
まとめ

この研究は,ビタミンB12依存メチル転送に不可欠な大きな酵素複合体の完全な構造を明らかにしています. コファクターを視覚化します.

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Hybrid Ensemble and Single-molecule Assay to Image the Motion of Fully Reconstituted CMG

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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
  • 酵素学 酵素学とは

背景:

  • ビタミンB12の誘導体は,重要な生物学的プロセスにおけるメチル基移転に不可欠です.
  • 既存の構造データは,関連する大型酵素複合体の断片のみをカバーしていました.

研究 の 目的:

  • B12依存メチル転送酵素複合体の完全な3次元構造を提示する.
  • カタリシス中のコファクターの動きとタンパク質の構造変化を視覚化します.

主な方法:

  • Moorella thermoaceticaからの完全な220 kDaの酵素複合体のX線結晶学.
  • 酵素活性を確認するために,イン・クリスタル光学分析.

主要な成果:

  • コリノイド鉄硫黄タンパク質とメチルトランスフェラーゼ複合体の最初の完全な3D構造.
  • ビタミンB12を複数の位置で可視化し,タンパク質の再編成とコファクターの軌道を明らかにします.
  • 結晶内の重要なタンパク質構成の変化を実証し,活性性を確認しました.

結論:

  • B12依存メチル転移の分子機構の構造モデルを提供します.
  • この重要な生物学的反応のために複雑なタンパク質機構の必要性を説明します.
  • 結晶状態で知られている最大のタンパク質構成の動きを強調しています.