1r5z

<StructureSection load='1r5z' size='340' side='right' caption='[[1r5z]], [[Resolution|resolution]] 1.95&Aring;' scene=''>

<table><tr><td colspan='2'>[[1r5z]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R5Z FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r5z OCA], [http://pdbe.org/1r5z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r5z RCSB], [http://www.ebi.ac.uk/pdbsum/1r5z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r5z ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/VATC_THET8 VATC_THET8]] Produces ATP from ADP in the presence of a proton gradient across the membrane.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The vacuole-type ATPases (V-ATPases) exist in various intracellular compartments of eukaryotic cells to regulate physiological processes by controlling the acidic environment. The crystal structure of the subunit C of Thermus thermophilus V-ATPase, homologous to eukaryotic subunit d of V-ATPases, has been determined at 1.95-A resolution and located into the holoenzyme complex structure obtained by single particle analysis as suggested by the results of subunit cross-linking experiments. The result shows that V-ATPase is substantially longer than the related F-type ATPase, due to the insertion of subunit C between the V(1) (soluble) and the V(o) (membrane bound) domains. Subunit C, attached to the V(o) domain, seems to have a socket like function in attaching the central-stalk subunits of the V(1) domain. This architecture seems essential for the reversible association/dissociation of the V(1) and the V(o) domains, unique for V-ATPase activity regulation.

Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase.,Iwata M, Imamura H, Stambouli E, Ikeda C, Tamakoshi M, Nagata K, Makyio H, Hankamer B, Barber J, Yoshida M, Yokoyama K, Iwata S Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):59-64. Epub 2003 Dec 18. PMID:14684831<ref>PMID:14684831</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1r5z" style="background-color:#fffaf0;"></div>

*[[ATPase|ATPase]]

[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]

[[Category: Barber, J]]

[[Category: Hankamer, B]]

[[Category: Ikeda, C]]

[[Category: Imamura, H]]

[[Category: Iwata, M]]

[[Category: Iwata, S]]

[[Category: Makyio, H]]

[[Category: Nagata, K]]

[[Category: Stambouli, E]]

[[Category: Tamakoshi, M]]

[[Category: Yokoyama, K]]

[[Category: Yoshida, M]]

[[Category: Hydrolase]]