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4xd7

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Revision as of 07:45, 7 October 2015

Structure of thermophilic F1-ATPase inhibited by epsilon subunit

Structural highlights

4xd7 is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ATPE_GEOKA] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530] [ATPA_GEOKA] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. [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. [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.

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shirakihara Y, Shiratori A, Tanikawa H, Nakasako M, Yoshida M, Suzuki T. Structure of a thermophilic F1 -ATPase inhibited by an epsilon-subunit: deeper insight into the epsilon-inhibition mechanism. FEBS J. 2015 Aug;282(15):2895-913. doi: 10.1111/febs.13329. Epub 2015 Jun 19. PMID:26032434 doi:http://dx.doi.org/10.1111/febs.13329

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xd7"

@@ Line 6: / Line 6: @@
 <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>
+<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://pdbe.org/4xd7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xd7 RCSB], [http://www.ebi.ac.uk/pdbsum/4xd7 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4xd7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4xd7

From Proteopedia

Revision as of 07:45, 7 October 2015

Structure of thermophilic F1-ATPase inhibited by epsilon subunit

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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