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Literature DB >> 24838125

NMR structures of α-proteobacterial ATPase-regulating ζ-subunits.

Pedro Serrano¹, Michael Geralt², Biswaranjan Mohanty³, Kurt Wüthrich³.

Abstract

NMR structures of ζ-subunits, which are recently discovered α-proteobacterial F1F0-ATPase-regulatory proteins representing a Pfam protein family of 246 sequences from 219 species (PF07345), exhibit a four-helix bundle, which is different from all other known F1F0-ATPase inhibitors. Chemical shift mapping reveals a conserved ADP/ATP binding site in ζ-subunit, which mediates long-range conformational changes related to function, as revealed by the structure of the Paracoccus denitrificans ζ-subunit in complex with ADP. These structural data suggest a new mechanism of F1F0-ATPase regulation in α-proteobacteria.

Entities: Chemical Disease Gene Species

Keywords: ATPase-regulating protein; NMR structure determination; PF07345; α-proteobacteria; ζ-subunit

Mesh：

Substances：

Year: 2014 PMID： 24838125 PMCID： PMC4089900 DOI： 10.1016/j.jmb.2014.05.004

Source DB: PubMed Journal: J Mol Biol ISSN： 0022-2836 Impact factor: 5.469

19 in total

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Journal: Curr Opin Struct Biol Date: 2002-10 Impact factor: 6.809

3. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.

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4. Automated sequence-specific protein NMR assignment using the memetic algorithm MATCH.

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5. The ζ subunit of the F1FO-ATP synthase of α-proteobacteria controls rotation of the nanomotor with a different structure.

Authors: Mariel Zarco-Zavala; Edgar Morales-Ríos; Guillermo Mendoza-Hernández; Leticia Ramírez-Silva; Gerardo Pérez-Hernández; José J García-Trejo
Journal: FASEB J Date: 2014-02-12 Impact factor: 5.191

6. Torsion angle dynamics for NMR structure calculation with the new program DYANA.

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Journal: J Mol Biol Date: 1997-10-17 Impact factor: 5.469

7. The J-UNIO protocol for automated protein structure determination by NMR in solution.

Authors: Pedro Serrano; Bill Pedrini; Biswaranjan Mohanty; Michael Geralt; Torsten Herrmann; Kurt Wüthrich
Journal: J Biomol NMR Date: 2012-07-03 Impact factor: 2.835

8. A novel 11-kDa inhibitory subunit in the F1FO ATP synthase of Paracoccus denitrificans and related alpha-proteobacteria.

Authors: Edgar Morales-Ríos; Fernanda de la Rosa-Morales; Guillermo Mendoza-Hernández; José S Rodríguez-Zavala; Heliodoro Celis; Mariel Zarco-Zavala; José J García-Trejo
Journal: FASEB J Date: 2009-09-25 Impact factor: 5.191

9. Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites.

Authors: Pedro Serrano; Bill Pedrini; Michael Geralt; Kristaps Jaudzems; Biswaranjan Mohanty; Reto Horst; Torsten Herrmann; Marc André Elsliger; Ian A Wilson; Kurt Wüthrich
Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun Date: 2010-09-30

10. Structures of the thermophilic F1-ATPase epsilon subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1.

Authors: Hiromasa Yagi; Nobumoto Kajiwara; Hideaki Tanaka; Tomitake Tsukihara; Yasuyuki Kato-Yamada; Masasuke Yoshida; Hideo Akutsu
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12 in total

1. Structure of ATP synthase from Paracoccus denitrificans determined by X-ray crystallography at 4.0 Å resolution.

Authors: Edgar Morales-Rios; Martin G Montgomery; Andrew G W Leslie; John E Walker
Journal: Proc Natl Acad Sci U S A Date: 2015-10-12 Impact factor: 11.205

Review 2. Control of rotation of the F₁F_O-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF₁ proteins.

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Journal: J Bioenerg Biomembr Date: 2018-09-28 Impact factor: 2.945

3. NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.

Authors: Pedro Serrano; Samit K Dutta; Andrew Proudfoot; Biswaranjan Mohanty; Lukas Susac; Bryan Martin; Michael Geralt; Lukasz Jaroszewski; Adam Godzik; Marc Elsliger; Ian A Wilson; Kurt Wüthrich
Journal: FEBS J Date: 2016-06-09 Impact factor: 5.542

4. J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.

Authors: Kristaps Jaudzems; Bill Pedrini; Michael Geralt; Pedro Serrano; Kurt Wüthrich
Journal: J Biomol NMR Date: 2014-11-27 Impact factor: 2.835

5. The Inhibitory Mechanism of the ζ Subunit of the F1FO-ATPase Nanomotor of Paracoccus denitrificans and Related α-Proteobacteria.

Authors: José J García-Trejo; Mariel Zarco-Zavala; Francisco Mendoza-Hoffmann; Eduardo Hernández-Luna; Raquel Ortega; Guillermo Mendoza-Hernández
Journal: J Biol Chem Date: 2015-11-06 Impact factor: 5.157

6. Purification, characterization and crystallization of the F-ATPase from Paracoccus denitrificans.

Authors: Edgar Morales-Rios; Ian N Watt; Qifeng Zhang; Shujing Ding; Ian M Fearnley; Martin G Montgomery; Michael J O Wakelam; John E Walker
Journal: Open Biol Date: 2015-09 Impact factor: 6.411

7. Deleting the IF₁-like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis.

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8. Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.

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9. Structure of a catalytic dimer of the α- and β-subunits of the F-ATPase from Paracoccus denitrificans at 2.3 Å resolution.

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Journal: Acta Crystallogr F Struct Biol Commun Date: 2015-09-23 Impact factor: 1.056

Review 10. Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.

Authors: Alexander Krah; Mariel Zarco-Zavala; Duncan G G McMillan
Journal: Open Biol Date: 2018-05 Impact factor: 6.411

Review 2. NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis.

Review 2. Control of rotation of the F1FO-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF1 proteins.

Review 10. Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.

Review 2. Control of rotation of the F₁F_O-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF₁ proteins.