View in EDS PDF Full Text

Crystal structure of a membrane-embedded H+-translocating pyrophosphatase.

Saved in:
Bibliographic Details
Title: Crystal structure of a membrane-embedded H+-translocating pyrophosphatase.
Authors: Lin, Shih-Ming, Tsai, Jia-Yin, Hsiao, Chwan-Deng, Huang, Yun-Tzu, Chiu, Chen-Liang, Liu, Mu-Hsuan, Tung, Jung-Yu, Liu, Tseng-Huang, Pan, Rong-Long, Sun, Yuh-Ju
Source: Nature. 4/19/2012, Vol. 484 Issue 7394, p399-403. 5p. 3 Color Photographs, 1 Diagram.
Subjects: Crystal structure, Pyrophosphates, Proton transfer reactions, Hydrolysis, Cell membranes
Abstract: H+-translocating pyrophosphatases (H+-PPases) are active proton transporters that establish a proton gradient across the endomembrane by means of pyrophosphate (PPi) hydrolysis. H+-PPases are found primarily as homodimers in the vacuolar membrane of plants and the plasma membrane of several protozoa and prokaryotes. The three-dimensional structure and detailed mechanisms underlying the enzymatic and proton translocation reactions of H+-PPases are unclear. Here we report the crystal structure of a Vigna radiata H+-PPase (VrH+-PPase) in complex with a non-hydrolysable substrate analogue, imidodiphosphate (IDP), at 2.35?Å resolution. Each VrH+-PPase subunit consists of an integral membrane domain formed by 16 transmembrane helices. IDP is bound in the cytosolic region of each subunit and trapped by numerous charged residues and five Mg2+ ions. A previously undescribed proton translocation pathway is formed by six core transmembrane helices. Proton pumping can be initialized by PPi hydrolysis, and H+ is then transported into the vacuolar lumen through a pathway consisting of Arg?242, Asp?294, Lys?742 and Glu?301. We propose a working model of the mechanism for the coupling between proton pumping and PPi hydrolysis by H+-PPases. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
FullText Links:
  – Type: pdflink
Text:
  Availability: 0
Header DbId: pbh
DbLabel: Psychology and Behavioral Sciences Collection
An: 74436370
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Crystal structure of a membrane-embedded H<superscript>+</superscript>-translocating pyrophosphatase.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Lin%2C+Shih-Ming%22">Lin, Shih-Ming</searchLink><br /><searchLink fieldCode="AR" term="%22Tsai%2C+Jia-Yin%22">Tsai, Jia-Yin</searchLink><br /><searchLink fieldCode="AR" term="%22Hsiao%2C+Chwan-Deng%22">Hsiao, Chwan-Deng</searchLink><br /><searchLink fieldCode="AR" term="%22Huang%2C+Yun-Tzu%22">Huang, Yun-Tzu</searchLink><br /><searchLink fieldCode="AR" term="%22Chiu%2C+Chen-Liang%22">Chiu, Chen-Liang</searchLink><br /><searchLink fieldCode="AR" term="%22Liu%2C+Mu-Hsuan%22">Liu, Mu-Hsuan</searchLink><br /><searchLink fieldCode="AR" term="%22Tung%2C+Jung-Yu%22">Tung, Jung-Yu</searchLink><br /><searchLink fieldCode="AR" term="%22Liu%2C+Tseng-Huang%22">Liu, Tseng-Huang</searchLink><br /><searchLink fieldCode="AR" term="%22Pan%2C+Rong-Long%22">Pan, Rong-Long</searchLink><br /><searchLink fieldCode="AR" term="%22Sun%2C+Yuh-Ju%22">Sun, Yuh-Ju</searchLink>
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 4/19/2012, Vol. 484 Issue 7394, p399-403. 5p. 3 Color Photographs, 1 Diagram.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Crystal+structure%22">Crystal structure</searchLink><br /><searchLink fieldCode="DE" term="%22Pyrophosphates%22">Pyrophosphates</searchLink><br /><searchLink fieldCode="DE" term="%22Proton+transfer+reactions%22">Proton transfer reactions</searchLink><br /><searchLink fieldCode="DE" term="%22Hydrolysis%22">Hydrolysis</searchLink><br /><searchLink fieldCode="DE" term="%22Cell+membranes%22">Cell membranes</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: H+-translocating pyrophosphatases (H+-PPases) are active proton transporters that establish a proton gradient across the endomembrane by means of pyrophosphate (PPi) hydrolysis. H+-PPases are found primarily as homodimers in the vacuolar membrane of plants and the plasma membrane of several protozoa and prokaryotes. The three-dimensional structure and detailed mechanisms underlying the enzymatic and proton translocation reactions of H+-PPases are unclear. Here we report the crystal structure of a Vigna radiata H+-PPase (VrH+-PPase) in complex with a non-hydrolysable substrate analogue, imidodiphosphate (IDP), at 2.35?Å resolution. Each VrH+-PPase subunit consists of an integral membrane domain formed by 16 transmembrane helices. IDP is bound in the cytosolic region of each subunit and trapped by numerous charged residues and five Mg2+ ions. A previously undescribed proton translocation pathway is formed by six core transmembrane helices. Proton pumping can be initialized by PPi hydrolysis, and H+ is then transported into the vacuolar lumen through a pathway consisting of Arg?242, Asp?294, Lys?742 and Glu?301. We propose a working model of the mechanism for the coupling between proton pumping and PPi hydrolysis by H+-PPases. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=74436370
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1038/nature10963
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 5
        StartPage: 399
    Subjects:
      – SubjectFull: Crystal structure
        Type: general
      – SubjectFull: Pyrophosphates
        Type: general
      – SubjectFull: Proton transfer reactions
        Type: general
      – SubjectFull: Hydrolysis
        Type: general
      – SubjectFull: Cell membranes
        Type: general
    Titles:
      – TitleFull: Crystal structure of a membrane-embedded H+-translocating pyrophosphatase.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Lin, Shih-Ming
      – PersonEntity:
          Name:
            NameFull: Tsai, Jia-Yin
      – PersonEntity:
          Name:
            NameFull: Hsiao, Chwan-Deng
      – PersonEntity:
          Name:
            NameFull: Huang, Yun-Tzu
      – PersonEntity:
          Name:
            NameFull: Chiu, Chen-Liang
      – PersonEntity:
          Name:
            NameFull: Liu, Mu-Hsuan
      – PersonEntity:
          Name:
            NameFull: Tung, Jung-Yu
      – PersonEntity:
          Name:
            NameFull: Liu, Tseng-Huang
      – PersonEntity:
          Name:
            NameFull: Pan, Rong-Long
      – PersonEntity:
          Name:
            NameFull: Sun, Yuh-Ju
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 19
              M: 04
              Text: 4/19/2012
              Type: published
              Y: 2012
          Identifiers:
            – Type: issn-print
              Value: 00280836
          Numbering:
            – Type: volume
              Value: 484
            – Type: issue
              Value: 7394
          Titles:
            – TitleFull: Nature
              Type: main
ResultId 1