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4mjn

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Revision as of 15:49, 4 August 2016

Structure of the c ring of the CF1FO ATP synthases.

Structural highlights

4mjn is a 14 chain structure with sequence from Triticum aestivum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2w5j
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ATPH_WHEAT] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits (By similarity).

Publication Abstract from PubMed

In eukaryotic- and prokaryotic cells F-ATP synthases provide energy through the synthesis of adenosine triphosphate (ATP). The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b' and c. Subunit c with a stoichiometry of 14 and subunit a form the gate for H+-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector. Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a = 144.420, b = 99.295, c = 123.51 A, and beta = 104.34 masculine and diffracted to 4.5 A resolution. Each c-ring contains fourteen monomers in the asymmetric unit. The length of the c-ring is 60.32 A, with an outer ring diameter 52.30 A, and an inner ring width of 40 A.

Crystallographic structure of the turbine c-ring from spinach chloroplast F-ATP synthase.,Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G Biosci Rep. 2014 Feb 13. PMID:24521269^[1]

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

References

↑ Balakrishna AM, Seelert H, Marx SH, Dencher NA, Gruber G. Crystallographic structure of the turbine c-ring from spinach chloroplast F-ATP synthase. Biosci Rep. 2014 Feb 13. PMID:24521269 doi:http://dx.doi.org/10.1042/BSR20130114

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Triticum aestivum | Balakrishna, A M | Gruber, G | Hydrolase

@@ Line 1: / Line 1: @@
 ==Structure of the c ring of the CF1FO ATP synthases.==
 <StructureSection load='4mjn' size='340' side='right' caption='[[4mjn]], [[Resolution|resolution]] 6.00&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2w5j|2w5j]]</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=4mjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mjn RCSB], [http://www.ebi.ac.uk/pdbsum/4mjn 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=4mjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mjn OCA], [http://pdbe.org/4mjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mjn RCSB], [http://www.ebi.ac.uk/pdbsum/4mjn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mjn ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4mjn" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase|ATPase]]
 == References ==
 <references/>

4mjn

From Proteopedia

Revision as of 15:49, 4 August 2016

Structure of the c ring of the CF1FO ATP synthases.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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