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1u7l

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(New page: 200px<br /><applet load="1u7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u7l, resolution 1.75&Aring;" /> '''Crystal Structure of...)
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[[Image:1u7l.jpg|left|200px]]<br /><applet load="1u7l" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u7l, resolution 1.75&Aring;" />
caption="1u7l, resolution 1.75&Aring;" />
'''Crystal Structure of subunit C (vma5p) of the yeast V-ATPase'''<br />
'''Crystal Structure of subunit C (vma5p) of the yeast V-ATPase'''<br />
==Overview==
==Overview==
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Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system, of eukaryotic cells. It provides most of the energy required for transport, systems that utilize the proton-motive force that is generated by ATP, hydrolysis. Some, but not all, of the V-ATPase subunits are homologous to, those of F-ATPase and the nonhomologous subunits determine the unique, features of V-ATPase. We determined the crystal structure of V-ATPase, subunit C (Vma5p), which does not show any homology with F-ATPase, subunits, at 1.75 A resolution. The structural features suggest that, subunit C functions as a flexible stator that holds together the catalytic, and membrane sectors of the enzyme. A second crystal form that was solved, at 2.9 A resolution supports the flexible nature of subunit C. These, structures provide a framework for exploring the unique mechanistic, features of V-ATPases.
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Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system of eukaryotic cells. It provides most of the energy required for transport systems that utilize the proton-motive force that is generated by ATP hydrolysis. Some, but not all, of the V-ATPase subunits are homologous to those of F-ATPase and the nonhomologous subunits determine the unique features of V-ATPase. We determined the crystal structure of V-ATPase subunit C (Vma5p), which does not show any homology with F-ATPase subunits, at 1.75 A resolution. The structural features suggest that subunit C functions as a flexible stator that holds together the catalytic and membrane sectors of the enzyme. A second crystal form that was solved at 2.9 A resolution supports the flexible nature of subunit C. These structures provide a framework for exploring the unique mechanistic features of V-ATPases.
==About this Structure==
==About this Structure==
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1U7L 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 TLA 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=1U7L OCA].
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1U7L 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=TLA:'>TLA</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=1U7L OCA].
==Reference==
==Reference==
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:54:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:27 2008''

Revision as of 13:21, 21 February 2008


1u7l, resolution 1.75Å

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Crystal Structure of subunit C (vma5p) of the yeast V-ATPase

Overview

Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system of eukaryotic cells. It provides most of the energy required for transport systems that utilize the proton-motive force that is generated by ATP hydrolysis. Some, but not all, of the V-ATPase subunits are homologous to those of F-ATPase and the nonhomologous subunits determine the unique features of V-ATPase. We determined the crystal structure of V-ATPase subunit C (Vma5p), which does not show any homology with F-ATPase subunits, at 1.75 A resolution. The structural features suggest that subunit C functions as a flexible stator that holds together the catalytic and membrane sectors of the enzyme. A second crystal form that was solved at 2.9 A resolution supports the flexible nature of subunit C. These structures provide a framework for exploring the unique mechanistic features of V-ATPases.

About this Structure

1U7L 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 yeast V-ATPase subunit C reveals its stator function., Drory O, Frolow F, Nelson N, EMBO Rep. 2004 Dec;5(12):1148-52. PMID:15540116

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