2nvj
From Proteopedia
(New page: 200px<br /><applet load="2nvj" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nvj" /> '''NMR structures of transmembrane segment from...) |
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==Overview== | ==Overview== | ||
| - | A 900-MHz NMR study is reported of peptide sMTM7 that mimics the | + | A 900-MHz NMR study is reported of peptide sMTM7 that mimics the cytoplasmic proton hemi-channel domain of the seventh transmembrane segment (TM7) from subunit a of H(+)-V-ATPase from Saccharomyces cerevisiae. The peptide encompasses the amino acid residues known to actively participate in proton translocation. In addition, peptide sMTM7 contains the amino acid residues that upon mutation cause V-ATPase to become resistant against the inhibitor bafilomycin. 2D TOCSY and NOESY (1)H-(1)H NMR spectra are obtained of sMTM7 dissolved in d(6)-DMSO and are used to calculate the three-dimensional structure of the peptide. The NMR-based structures and corresponding dynamical features of peptide sMTM7 show that sMTM7 is composed of two alpha-helical regions. These regions are separated by a flexible hinge of two residues. The hinge acts as a ball-and-joint socket and both helical segments move independently with respect to one another. This movement in TM7 is suggested to cause the opening and closing of the cytoplasmic proton hemi-channel and enables proton translocation. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Segment TM7 from the cytoplasmic hemi-channel from | + | Segment TM7 from the cytoplasmic hemi-channel from VO-H+-V-ATPase includes a flexible region that has a potential role in proton translocation., Duarte AM, de Jong ER, Wechselberger R, van Mierlo CP, Hemminga MA, Biochim Biophys Acta. 2007 Sep;1768(9):2263-70. Epub 2007 May 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17573038 17573038] |
[[Category: H(+)-transporting two-sector ATPase]] | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Duarte, A | + | [[Category: Duarte, A M.]] |
| - | [[Category: Hemminga, M | + | [[Category: Hemminga, M A.]] |
| - | [[Category: Jong, E | + | [[Category: Jong, E R.de.]] |
| - | [[Category: Mierlo, C | + | [[Category: Mierlo, C P.van.]] |
[[Category: Wechselberger, R.]] | [[Category: Wechselberger, R.]] | ||
[[Category: 10 helix]] | [[Category: 10 helix]] | ||
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[[Category: pi helix]] | [[Category: pi helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:11:30 2008'' |
Revision as of 16:11, 21 February 2008
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NMR structures of transmembrane segment from subunit a from the yeast proton V-ATPase
Overview
A 900-MHz NMR study is reported of peptide sMTM7 that mimics the cytoplasmic proton hemi-channel domain of the seventh transmembrane segment (TM7) from subunit a of H(+)-V-ATPase from Saccharomyces cerevisiae. The peptide encompasses the amino acid residues known to actively participate in proton translocation. In addition, peptide sMTM7 contains the amino acid residues that upon mutation cause V-ATPase to become resistant against the inhibitor bafilomycin. 2D TOCSY and NOESY (1)H-(1)H NMR spectra are obtained of sMTM7 dissolved in d(6)-DMSO and are used to calculate the three-dimensional structure of the peptide. The NMR-based structures and corresponding dynamical features of peptide sMTM7 show that sMTM7 is composed of two alpha-helical regions. These regions are separated by a flexible hinge of two residues. The hinge acts as a ball-and-joint socket and both helical segments move independently with respect to one another. This movement in TM7 is suggested to cause the opening and closing of the cytoplasmic proton hemi-channel and enables proton translocation.
About this Structure
2NVJ is a Single protein structure of sequence from [1]. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
Segment TM7 from the cytoplasmic hemi-channel from VO-H+-V-ATPase includes a flexible region that has a potential role in proton translocation., Duarte AM, de Jong ER, Wechselberger R, van Mierlo CP, Hemminga MA, Biochim Biophys Acta. 2007 Sep;1768(9):2263-70. Epub 2007 May 21. PMID:17573038
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