4CI0

Electron cryo-microscopy of F420-reducing NiFe hydrogenase Frh

4CI0 の概要

• エントリーDOI: 10.2210/pdb4ci0/pdb
• EMDBエントリー: 2513
• 分子名称: F420-REDUCING HYDROGENASE, SUBUNIT ALPHA, F420-REDUCING HYDROGENASE, SUBUNIT GAMMA, F420-REDUCING HYDROGENASE, SUBUNIT BETA, ... (9 entities in total)
• 機能のキーワード: oxidoreductase, flavoprotein, electron transfer, ferredoxin
• 由来する生物種: METHANOTHERMOBACTER MARBURGENSIS; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 106171.19

構造登録者

Allegretti, M.,Mills, D.J.,McMullan, G.,Kuehlbrandt, W.,Vonck, J. (登録日: 2013-12-05, 公開日: 2014-02-26, 最終更新日: 2024-11-06)

主引用文献

Allegretti, M.,Mills, D.J.,Mcmullan, G.,Kuehlbrandt, W.,Vonck, J.
Atomic Model of the F420-Reducing [Nife] Hydrogenase by Electron Cryo-Electron Microscopy Using a Direct Electron Detector.
Elife, 3:01963-, 2014

PubMed Abstract: The introduction of direct electron detectors with higher detective quantum efficiency and fast read-out marks the beginning of a new era in electron cryo-microscopy. Using the FEI Falcon II direct electron detector in video mode, we have reconstructed a map at 3.36 Å resolution of the 1.2 MDa F420-reducing hydrogenase (Frh) from methanogenic archaea from only 320,000 asymmetric units. Videos frames were aligned by a combination of image and particle alignment procedures to overcome the effects of beam-induced motion. The reconstructed density map shows all secondary structure as well as clear side chain densities for most residues. The full coordination of all cofactors in the electron transfer chain (a [NiFe] center, four [4Fe4S] clusters and an FAD) is clearly visible along with a well-defined substrate access channel. From the rigidity of the complex we conclude that catalysis is diffusion-limited and does not depend on protein flexibility or conformational changes. DOI: http://dx.doi.org/10.7554/eLife.01963.001.

PubMed: 24569482
DOI: 10.7554/ELIFE.01963

実験手法

ELECTRON MICROSCOPY (3.36 Å)