1v9m
From Proteopedia
(New page: 200px<br /><applet load="1v9m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v9m, resolution 1.85Å" /> '''Crystal structure of...) |
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| - | [[Image:1v9m.jpg|left|200px]]<br /><applet load="1v9m" size=" | + | [[Image:1v9m.jpg|left|200px]]<br /><applet load="1v9m" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1v9m, resolution 1.85Å" /> | caption="1v9m, resolution 1.85Å" /> | ||
'''Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus'''<br /> | '''Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The V-type H(+)-ATPases are similar to the F-type ATP synthases in their | + | The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft. |
==About this Structure== | ==About this Structure== | ||
| - | 1V9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with GOL 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:// | + | 1V9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=GOL:'>GOL</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=1V9M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
[[Category: Numoto, N.]] | [[Category: Numoto, N.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
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[[Category: vov1-atpase]] | [[Category: vov1-atpase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:05 2008'' |
Revision as of 13:33, 21 February 2008
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Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus
Overview
The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft.
About this Structure
1V9M is a Single protein structure of sequence from Thermus thermophilus 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
Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution., Numoto N, Kita A, Miki K, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:15103125
Page seeded by OCA on Thu Feb 21 15:33:05 2008
Categories: H(+)-transporting two-sector ATPase | Single protein | Thermus thermophilus | Kita, A. | Miki, K. | Numoto, N. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | GOL | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | The c subunit | V-type atpase | Vov1-atpase
