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| [[Image:1ho8.jpg|left|200px]] | | {{Seed}} |
| | [[Image:1ho8.png|left|200px]] |
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| {{STRUCTURE_1ho8| PDB=1ho8 | SCENE= }} | | {{STRUCTURE_1ho8| PDB=1ho8 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE'''
| | ===CRYSTAL STRUCTURE OF THE REGULATORY SUBUNIT H OF THE V-TYPE ATPASE OF SACCHAROMYCES CEREVISIAE=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11416198}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11416198 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11416198}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Stevens, T H.]] | | [[Category: Stevens, T H.]] |
| [[Category: Heat repeat]] | | [[Category: Heat repeat]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:03:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:27:52 2008'' |