4xd7: Difference between revisions

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-'''Unreleased structure'''
+==Structure of thermophilic F1-ATPase inhibited by epsilon subunit==
+<StructureSection load='4xd7' size='340' side='right' caption='[[4xd7]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4xd7]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XD7 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4xd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xd7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xd7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xd7 PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ATPE_GEOKA ATPE_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530] [[http://www.uniprot.org/uniprot/ATPA_GEOKA ATPA_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. [[http://www.uniprot.org/uniprot/ATPG_GEOKA ATPG_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. [[http://www.uniprot.org/uniprot/ATPB_GEOKA ATPB_GEOKA]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+F1 -ATPase (F1 ) is the catalytic sector in Fo F1 -ATP synthase that is responsible for ATP production in living cells. In catalysis, its three catalytic beta-subunits undergo nucleotide occupancy-dependent and concerted open-close conformational changes that are accompanied by rotation of the gamma-subunit. Bacterial and chloroplast F1 are inhibited by their own epsilon-subunit. In the epsilon-inhibited Escherichia coli F1 structure, the epsilon-subunit stabilizes the overall conformation (half-closed, closed, open) of the beta-subunits by inserting its C-terminal helix into the alpha3 beta3 cavity. The structure of epsilon-inhibited thermophilic F1 is similar to that of E. coli F1 , showing a similar conformation of the epsilon-subunit, but the thermophilic epsilon-subunit stabilizes another unique overall conformation (open, closed, open) of the beta-subunits. The epsilon-C-terminal helix 2 and hook are conserved between the two structures in interactions with target residues and in their positions. Rest of the epsilon-C-terminal domains are in quite different conformations and positions, and have different modes of interaction with targets. This region is thought to serve epsilon-inhibition differently. For inhibition, the epsilon-subunit contacts the second catches of some of the beta- and alpha-subunits, the N- and C-terminal helices, and some of the Rossmann fold segments. Those contacts, as a whole, lead to positioning of those beta- and alpha- second catches in epsilon-inhibition-specific positions, and prevent rotation of the gamma-subunit. Some of the structural features are observed even in IF1 inhibition in mitochondrial F1 . DATABASE: Structural data are available in the Worldwide Protein Data Bank database under the accession number 4XD7.
-The entry 4xd7 is ON HOLD
+Structure of a thermophilic F1 -ATPase inhibited by an epsilon-subunit: deeper insight into the epsilon-inhibition mechanism.,Shirakihara Y, Shiratori A, Tanikawa H, Nakasako M, Yoshida M, Suzuki T FEBS J. 2015 Aug;282(15):2895-913. doi: 10.1111/febs.13329. Epub 2015 Jun 19. PMID:26032434<ref>PMID:26032434</ref>
-Authors: SHIRAKIHARA, Y., SHIRATORI, A., TANIKAWA, H., NAKASAKO, M., YOSHIDA, M., SUZUK, T.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Structure of thermophilic F1-ATPase inhibited by epsilon subunit
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Yoshida, M]]
+__TOC__
-[[Category: Shiratori, A]]
+</StructureSection>
-[[Category: Shirakihara, Y]]
+[[Category: NAKASAKO, M]]
-[[Category: Suzuk, T]]
+[[Category: SHIRAKIHARA, Y]]
-[[Category: Tanikawa, H]]
+[[Category: SHIRATORI, A]]
-[[Category: Nakasako, M]]
+[[Category: SUZUK, T]]
+[[Category: TANIKAWA, H]]
+[[Category: YOSHIDA, M]]
+[[Category: Atp synthase]]
+[[Category: Bacillus ps3]]
+[[Category: F1-atpase]]
+[[Category: Hydrolase]]
+[[Category: Rotary motor protein]]
+[[Category: Rotational catalysis]]
+[[Category: Thermophilic]]