1u7l: Difference between revisions
New page: left|200px<br /><applet load="1u7l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u7l, resolution 1.75Å" /> '''Crystal Structure of... |
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[[Image:1u7l.jpg|left|200px]]<br /><applet load="1u7l" size=" | [[Image:1u7l.jpg|left|200px]]<br /><applet load="1u7l" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1u7l, resolution 1.75Å" /> | caption="1u7l, resolution 1.75Å" /> | ||
'''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== | ||
Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system | 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== | ||
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:// | 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]] | ||
''Page seeded by [http:// | ''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
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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 TLA 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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