Journal of Molecular Biology
Improvement of the 2.5 Å resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics☆
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Cited by (128)
Recognizing asymmetry in pseudo-symmetry; structural insights into the interaction between amphipathic α-helices and X-bundle proteins
2017, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :One extremity of the apolipoprotein E3 four-helix bundle is highly mobile and undergoes minor conformational changes to expose the hydrophobic residues within the helical bundle to the acyl chains of lipids [53,68]. A region on the cytochrome b562 four-helix bundle in which two α-helices slightly splay apart creates a narrow binding pocket that accommodates the shape of a heme-containing porphyrin ring [37]. In another example, the granulocyte macrophage colony-stimulating factor (GM-CSF) contains an anti-parallel four-helix bundle organized as an X-helix bundle wherein two adjacent α-helices found on the exterior of the helical bundle form a binding platform for the GM-CFF receptor [13].
Reengineering cyt b<inf>562</inf> for hydrogen production: A facile route to artificial hydrogenases
2016, Biochimica et Biophysica Acta - BioenergeticsCitation Excerpt :Rates of hydrogen production were integrated to obtain moles of hydrogen produced, and utilized for calculation of final TON. We choose as scaffold for our investigation cyt b562, a 106-amino acid protein that folds into a stable, antiparallel four-helix bundle, and binds metallated protoporphyrin (IX) non-covalently through coordination by His107 and Met7 (Fig. 1) [34]. We characterized CoPP(IX) complex of wild type, and compared it to mutants that explore loss of coordination (M7A) or a switch to carboxylate as coordinating moiety (M7D and M7E) in order to investigate the effect of axial coordination on the properties of Co-cyt b562 [46,47].
Elastic rotation of Escherichia coli F<inf>O</inf>F<inf>1</inf> having ε subunit fused with cytochrome b<inf>562</inf> or flavodoxin reductase
2014, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Thus, it is difficult to assume that we observed rotations of the FOF1 from which modified ε was released. Crystal structures of the cytochrome b562 and the flavodoxin reductase have been determined, revealing molecular dimensions of 23 × 24 × 48 Å and 30 × 35 × 55 Å, respectively [27,28] (Fig. 1C). Although the precise space size between the two stalks connecting F1 and FO has not been defined, we estimated the spherical space with a diameter of about 30 Å from the electron cryo-microscopy of mitochondrial FOF1 [10] (Fig. 1B, shown by a red circle).
Fusion partner toolchest for the stabilization and crystallization of G protein-coupled receptors
2012, StructureCitation Excerpt :Thus, though the connection between receptor helix V and BRIL helix I are almost perfectly aligned, receptor helix VI connects with BRIL helix IV at an angle of ∼40°. This bending distortion is accommodated by the last two turns of helix IV in BRIL and is highly flexible in apocytochrome b562, as it exhibits large conformational variations between NMR models (Feng et al., 2004) as well as between crystal structures of the apo- and heme-bound cytochrome b562 (Lederer et al., 1981) (Figure 7C). Additionally, the long loop connecting helices II and III in the heme-binding region of BRIL has 16 disordered residues, which also reflects its highly flexible behavior described previously in apo-BRIL NMR studies.
Biomolecules under mechanical force
2010, Physics Reports
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This work has been supported in part by the Centre National de la Recherche Scientifique (ATP 3390), the Délégation Générale à la Recherche Scientifique et Technique and the Fondation pour la Recherche Médicale Française (to F. L.) and by the National Institutes of Health (grant no. G.M. 20530) and the National Science Foundation (grant no. PCM 79–22708, to F. S. M.). The collaborative nature of this investigation has been supported by a NATO research grant (no. 1107).