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6n30

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Revision as of 22:45, 6 March 2020

Bacillus PS3 ATP synthase class 3

6n30, resolution 3.20Å

Structural highlights

6n30 is a 22 chain structure with sequence from Bacp3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	6n2y, 6n2z, 6n2d
Gene:	atpE, uncE (BACP3), uncA, atpA (BACP3), uncD, atpD (BACP3), uncG, atpG (BACP3), uncC, atpC (BACP3)
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[A0A0M4U1P9_BACP3] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.[HAMAP-Rule:MF_01347] [A0A0M4TPJ7_BACP3] 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.[HAMAP-Rule:MF_00815][SAAS:SAAS00725627] [A0A0M5MQR7_BACP3] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530][SAAS:SAAS00872986] [ATPL_BACP3] 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.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] [A0A0M3VGF9_BACP3] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346]

Publication Abstract from PubMed

ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit epsilon shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme.

Structure of a bacterial ATP synthase.,Guo H, Suzuki T, Rubinstein JL Elife. 2019 Feb 6;8. pii: 43128. doi: 10.7554/eLife.43128. PMID:30724163^[1]

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

References

↑ Guo H, Suzuki T, Rubinstein JL. Structure of a bacterial ATP synthase. Elife. 2019 Feb 6;8. pii: 43128. doi: 10.7554/eLife.43128. PMID:30724163 doi:http://dx.doi.org/10.7554/eLife.43128

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/6n30"

@@ Line 1: / Line 1: @@
-{{Large structure}}
 ==Bacillus PS3 ATP synthase class 3==
-<StructureSection load='6n30' size='340' side='right' caption='[[6n30]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<SX load='6n30' size='340' side='right' viewer='molstar' caption='[[6n30]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6n30]] is a 22 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N30 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6n30]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacp3 Bacp3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N30 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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6n2y|6n2y]], [[6n2z|6n2z]], [[6n2d|6n2d]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">atpE, uncE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2334 BACP3]), uncA, atpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2334 BACP3]), uncD, atpD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2334 BACP3]), uncG, atpG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2334 BACP3]), uncC, atpC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2334 BACP3])</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=6n30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n30 OCA], [http://pdbe.org/6n30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n30 RCSB], [http://www.ebi.ac.uk/pdbsum/6n30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n30 ProSAT]</span></td></tr>
 </table>
-{{Large structure}}
 == Function ==
 [[http://www.uniprot.org/uniprot/A0A0M4U1P9_BACP3 A0A0M4U1P9_BACP3]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.[HAMAP-Rule:MF_01347] [[http://www.uniprot.org/uniprot/A0A0M4TPJ7_BACP3 A0A0M4TPJ7_BACP3]] 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.[HAMAP-Rule:MF_00815][SAAS:SAAS00725627] [[http://www.uniprot.org/uniprot/A0A0M5MQR7_BACP3 A0A0M5MQR7_BACP3]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530][SAAS:SAAS00872986] [[http://www.uniprot.org/uniprot/ATPL_BACP3 ATPL_BACP3]] 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.[HAMAP-Rule:MF_01396]  Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] [[http://www.uniprot.org/uniprot/A0A0M3VGF9_BACP3 A0A0M3VGF9_BACP3]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.[HAMAP-Rule:MF_01346]
@@ Line 25: / Line 25: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
+[[Category: Bacp3]]
+[[Category: Large Structures]]
 [[Category: Guo, H]]
 [[Category: Rubinstein, J L]]
 [[Category: Bacterial atp synthase]]
 [[Category: Hydrolase]]

6n30

From Proteopedia

Revision as of 22:45, 6 March 2020

Bacillus PS3 ATP synthase class 3

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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