Crystal structure of the central axis DF complex of the prokaryotic V-ATPase
V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal str...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2011-12, Vol.108 (50), p.19955-19960 |
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| creator | Saijo, Shinya Arai, Satoshi Hossain, K. M. Mozaffor Yamato, Ichiro Suzuki, Kano Kakinuma, Yoshimi Ishizuka-Katsura, Yoshiko Ohsawa, Noboru Terada, Takaho Shirouzu, Mikako Yokoyama, Shigeyuki Iwata, So Murata, Takeshi |
| description | V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-hairpin region that is effective in stimulating the ATPase activity of V1-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A3B3 complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase. |
| doi_str_mv | 10.1073/pnas.1108810108 |
| format | Article |
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M. Mozaffor ; Yamato, Ichiro ; Suzuki, Kano ; Kakinuma, Yoshimi ; Ishizuka-Katsura, Yoshiko ; Ohsawa, Noboru ; Terada, Takaho ; Shirouzu, Mikako ; Yokoyama, Shigeyuki ; Iwata, So ; Murata, Takeshi</creator><creatorcontrib>Saijo, Shinya ; Arai, Satoshi ; Hossain, K. M. Mozaffor ; Yamato, Ichiro ; Suzuki, Kano ; Kakinuma, Yoshimi ; Ishizuka-Katsura, Yoshiko ; Ohsawa, Noboru ; Terada, Takaho ; Shirouzu, Mikako ; Yokoyama, Shigeyuki ; Iwata, So ; Murata, Takeshi</creatorcontrib><description>V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-hairpin region that is effective in stimulating the ATPase activity of V1-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A3B3 complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1108810108</identifier><identifier>PMID: 22114184</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Adenosine triphosphatase ; Adenosine triphosphatases ; adenosine triphosphate ; adenosinetriphosphatase ; Amino Acid Sequence ; Archaea ; ATP ; Binding sites ; Biochemistry ; Biological Sciences ; Cell membranes ; Crystal structure ; Crystallography, X-Ray ; Enterococcus ; Enterococcus - enzymology ; Enterococcus hirae ; hydrolysis ; Membranes ; Models, Molecular ; Molecular Sequence Data ; Physiology ; Prokaryotes ; Prokaryotic Cells - enzymology ; Protein Structure, Secondary ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; Proteins ; Rotation ; Sequence Alignment ; Static Electricity ; Structural Homology, Protein ; Thermus ; transporters ; Vacuolar Proton-Translocating ATPases - chemistry ; Vacuolar Proton-Translocating ATPases - metabolism</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2011-12, Vol.108 (50), p.19955-19960</ispartof><rights>copyright © 1993—2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Dec 13, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c589t-8f0aa4bf8f8d8eeee9a31ce797c29ff1769da427ab7f0a6cded2c22738c8daee3</citedby><cites>FETCH-LOGICAL-c589t-8f0aa4bf8f8d8eeee9a31ce797c29ff1769da427ab7f0a6cded2c22738c8daee3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/108/50.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23060057$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23060057$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22114184$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Saijo, Shinya</creatorcontrib><creatorcontrib>Arai, Satoshi</creatorcontrib><creatorcontrib>Hossain, K. M. Mozaffor</creatorcontrib><creatorcontrib>Yamato, Ichiro</creatorcontrib><creatorcontrib>Suzuki, Kano</creatorcontrib><creatorcontrib>Kakinuma, Yoshimi</creatorcontrib><creatorcontrib>Ishizuka-Katsura, Yoshiko</creatorcontrib><creatorcontrib>Ohsawa, Noboru</creatorcontrib><creatorcontrib>Terada, Takaho</creatorcontrib><creatorcontrib>Shirouzu, Mikako</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</creatorcontrib><creatorcontrib>Iwata, So</creatorcontrib><creatorcontrib>Murata, Takeshi</creatorcontrib><title>Crystal structure of the central axis DF complex of the prokaryotic V-ATPase</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-hairpin region that is effective in stimulating the ATPase activity of V1-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A3B3 complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.</description><subject>Adenosine triphosphatase</subject><subject>Adenosine triphosphatases</subject><subject>adenosine triphosphate</subject><subject>adenosinetriphosphatase</subject><subject>Amino Acid Sequence</subject><subject>Archaea</subject><subject>ATP</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Cell membranes</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Enterococcus</subject><subject>Enterococcus - enzymology</subject><subject>Enterococcus hirae</subject><subject>hydrolysis</subject><subject>Membranes</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Physiology</subject><subject>Prokaryotes</subject><subject>Prokaryotic Cells - enzymology</subject><subject>Protein Structure, Secondary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - metabolism</subject><subject>Proteins</subject><subject>Rotation</subject><subject>Sequence Alignment</subject><subject>Static Electricity</subject><subject>Structural Homology, Protein</subject><subject>Thermus</subject><subject>transporters</subject><subject>Vacuolar Proton-Translocating ATPases - chemistry</subject><subject>Vacuolar Proton-Translocating ATPases - metabolism</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9ks1v1DAUxC0EokvhzAmIeimXtM9fsX1BqhZakFYCiZar5XWcNks2DnZStf89b7XbLnDAB_swvzcae0zIawonFBQ_HXqXTygFrSng_oTMKBhaVsLAUzIDYKrUgokD8iLnFQAYqeE5OWCMUkG1mJHFPN3n0XVFHtPkxymFIjbFeBMKH_oxoeDu2lx8PC98XA9duHuQhxR_unQfx9YXP8qzy28uh5fkWeO6HF7tzkNydf7pcv65XHy9-DI_W5ReajOWugHnxLLRja51wGUcpz4oozwzTUNVZWonmHJLhWTl61Azz5ji2uvahcAPyYet7zAt16HeJbVDatcYyUbX2r-Vvr2x1_HWciaBcooGxzuDFH9NIY923WYfus71IU7ZGkqN4Agi-f6_JJXcCClBVoge_YOu4pR6fAj0A6OwH0DodAv5FHNOoXlMTcFuKrWbSu2-Upx4--dlH_mHDhEodsBmcm-nrURLY6RE5M0WWeUxpr0FhwpAKtTfbfXGReuuU5vt1XcGVOCXqQyvGP8NiMS64Q</recordid><startdate>20111213</startdate><enddate>20111213</enddate><creator>Saijo, Shinya</creator><creator>Arai, Satoshi</creator><creator>Hossain, K. 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M. Mozaffor</au><au>Yamato, Ichiro</au><au>Suzuki, Kano</au><au>Kakinuma, Yoshimi</au><au>Ishizuka-Katsura, Yoshiko</au><au>Ohsawa, Noboru</au><au>Terada, Takaho</au><au>Shirouzu, Mikako</au><au>Yokoyama, Shigeyuki</au><au>Iwata, So</au><au>Murata, Takeshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of the central axis DF complex of the prokaryotic V-ATPase</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2011-12-13</date><risdate>2011</risdate><volume>108</volume><issue>50</issue><spage>19955</spage><epage>19960</epage><pages>19955-19960</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-Å resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short β-hairpin region that is effective in stimulating the ATPase activity of V1-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A3B3 complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>22114184</pmid><doi>10.1073/pnas.1108810108</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine triphosphatase Adenosine triphosphatases adenosine triphosphate adenosinetriphosphatase Amino Acid Sequence Archaea ATP Binding sites Biochemistry Biological Sciences Cell membranes Crystal structure Crystallography, X-Ray Enterococcus Enterococcus - enzymology Enterococcus hirae hydrolysis Membranes Models, Molecular Molecular Sequence Data Physiology Prokaryotes Prokaryotic Cells - enzymology Protein Structure, Secondary Protein Subunits - chemistry Protein Subunits - metabolism Proteins Rotation Sequence Alignment Static Electricity Structural Homology, Protein Thermus transporters Vacuolar Proton-Translocating ATPases - chemistry Vacuolar Proton-Translocating ATPases - metabolism |
| title | Crystal structure of the central axis DF complex of the prokaryotic V-ATPase |
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