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1ho8

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(New page: 200px<br /><applet load="1ho8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ho8, resolution 2.95&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1ho8.jpg|left|200px]]<br /><applet load="1ho8" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ho8.jpg|left|200px]]<br /><applet load="1ho8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ho8, resolution 2.95&Aring;" />
caption="1ho8, resolution 2.95&Aring;" />
'''CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE'''<br />
'''CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE'''<br />
==Overview==
==Overview==
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In contrast to the F-type ATPases, which use a proton gradient to generate, ATP, the V-type enzymes use ATP to actively transport protons into, organelles and extracellular compartments. We describe here the structure, of the H-subunit (also called Vma13p) of the yeast enzyme. This is the, first structure of any component of a V-type ATPase. The H-subunit is not, required for assembly but plays an essential regulatory role. Despite the, lack of any apparent sequence homology the structure contains five motifs, similar to the so-called HEAT or armadillo repeats seen in the importins., A groove, which is occupied in the importins by the peptide that targets, proteins for import into the nucleus, is occupied here by the 10, amino-terminal residues of subunit H itself. The structural similarity, suggests how subunit H may interact with the ATPase itself or with other, proteins. A cleft between the amino- and carboxyl-terminal domains also, suggests another possible site of interaction with other factors.
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In contrast to the F-type ATPases, which use a proton gradient to generate ATP, the V-type enzymes use ATP to actively transport protons into organelles and extracellular compartments. We describe here the structure of the H-subunit (also called Vma13p) of the yeast enzyme. This is the first structure of any component of a V-type ATPase. The H-subunit is not required for assembly but plays an essential regulatory role. Despite the lack of any apparent sequence homology the structure contains five motifs similar to the so-called HEAT or armadillo repeats seen in the importins. A groove, which is occupied in the importins by the peptide that targets proteins for import into the nucleus, is occupied here by the 10 amino-terminal residues of subunit H itself. The structural similarity suggests how subunit H may interact with the ATPase itself or with other proteins. A cleft between the amino- and carboxyl-terminal domains also suggests another possible site of interaction with other factors.
==About this Structure==
==About this Structure==
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1HO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HO8 OCA].
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1HO8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HO8 OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Matthews, B.W.]]
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[[Category: Matthews, B W.]]
[[Category: Sagermann, M.]]
[[Category: Sagermann, M.]]
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[[Category: Stevens, T.H.]]
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[[Category: Stevens, T H.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: heat repeat]]
[[Category: heat repeat]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:42:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:14 2008''

Revision as of 11:03, 21 February 2008


1ho8, resolution 2.95Å

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CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE

Overview

In contrast to the F-type ATPases, which use a proton gradient to generate ATP, the V-type enzymes use ATP to actively transport protons into organelles and extracellular compartments. We describe here the structure of the H-subunit (also called Vma13p) of the yeast enzyme. This is the first structure of any component of a V-type ATPase. The H-subunit is not required for assembly but plays an essential regulatory role. Despite the lack of any apparent sequence homology the structure contains five motifs similar to the so-called HEAT or armadillo repeats seen in the importins. A groove, which is occupied in the importins by the peptide that targets proteins for import into the nucleus, is occupied here by the 10 amino-terminal residues of subunit H itself. The structural similarity suggests how subunit H may interact with the ATPase itself or with other proteins. A cleft between the amino- and carboxyl-terminal domains also suggests another possible site of interaction with other factors.

About this Structure

1HO8 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.

Reference

Crystal structure of the regulatory subunit H of the V-type ATPase of Saccharomyces cerevisiae., Sagermann M, Stevens TH, Matthews BW, Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7134-9. PMID:11416198

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