(Q43675735)

English

Interaction and stoichiometry of the peripheral stalk subunits NtpE and NtpF and the N-terminal hydrophilic domain of NtpI of Enterococcus hirae V-ATPase.

scientific article published on 6 May 2008

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scholarly article

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7 January 2020

Interaction and stoichiometry of the peripheral stalk subunits NtpE and NtpF and the N-terminal hydrophilic domain of NtpI of Enterococcus hirae V-ATPase (English)

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7 January 2020

Enterococcus hirae

object named as

Enterococcus hirae

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inferred from title

Shigeyuki Yokoyama

14

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7 January 2020

Masaki Yamamoto

1

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7 January 2020

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7 January 2020

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Satoru Unzai

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7 January 2020

Shinya Saijo

3

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Kazuki Ito

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Kenji Mizutani

5

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7 January 2020

Chiyo Suno-Ikeda

6

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7 January 2020

Yukako Yabuki-Miyata

7

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7 January 2020

Takaho Terada

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Mitsutoshi Toyama

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Mikako Shirouzu

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7 January 2020

Takuya Kobayashi

11

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Yoshimi Kakinuma

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7 January 2020

Ichiro Yamato

13

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So Iwata

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publication date

6 May 2008

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7 January 2020

Journal of Biological Chemistry

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19422-19431

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7 January 2020

Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology

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Defined sites of interaction between subunits E (Vma4p), C (Vma5p), and G (Vma10p) within the stator structure of the vacuolar H+-ATPase.

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Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain

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V1 and V0 domains of the human H+-ATPase are linked by an interaction between the G and a subunits

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Building the stator of the yeast vacuolar-ATPase: specific interaction between subunits E and G.

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The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex

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Stoichiometry of the peripheral stalk subunits E and G of yeast V1-ATPase determined by mass spectrometry

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21 January 2018

Stoichiometry and localization of the stator subunits E and G in Thermus thermophilus H+-ATPase/synthase

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Rotation, structure, and classification of prokaryotic V-ATPase.

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Structure and mechanism of vacuolar Na+-translocating ATPase from Enterococcus hirae

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21 January 2018

Subunit composition, structure, and distribution of bacterial V-type ATPases

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21 January 2018

Catalytic properties of Na(+)-translocating V-ATPase in Enterococcus hirae

1 reference

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21 January 2018

Structure and function of vacuolar Na+-translocating ATPase in Enterococcus hirae

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21 January 2018

Novel vacuolar H+-ATPase complexes resulting from overproduction of Vma5p and Vma13p

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Structure of the rotor of the V-Type Na+-ATPase from Enterococcus hirae

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Arginine residue at position 573 in Enterococcus hirae vacuolar-type ATPase NtpI subunit plays a crucial role in Na+ translocation.

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21 January 2018

The stator complex of the A1A0-ATP synthase--structural characterization of the E and H subunits

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Modern applications of analytical ultracentrifugation

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21 January 2018

Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase

1 reference

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21 January 2018

ATP-dependent affinity change of Na+-binding sites of V-ATPase

1 reference

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21 January 2018

Identifiers

10.1074/JBC.M801772200

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7 January 2020

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7 January 2020

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