6q45: Difference between revisions

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<StructureSection load='6q45' size='340' side='right'caption='[[6q45]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='6q45' size='340' side='right'caption='[[6q45]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6q45]] is a 16 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q45 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q45 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6q45]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusobacterium_nucleatum_subsp._nucleatum_ATCC_25586 Fusobacterium nucleatum subsp. nucleatum ATCC 25586]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q45 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></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</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=6q45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q45 OCA], [http://pdbe.org/6q45 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q45 RCSB], [http://www.ebi.ac.uk/pdbsum/6q45 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q45 ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6q45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q45 OCA], [https://pdbe.org/6q45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q45 RCSB], [https://www.ebi.ac.uk/pdbsum/6q45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q45 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ATPE_FUSNN ATPE_FUSNN]] Produces ATP from ADP in the presence of a proton gradient across the membrane. [[http://www.uniprot.org/uniprot/ATPA_FUSNN ATPA_FUSNN]] 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_FUSNN ATPG_FUSNN]] 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_FUSNN ATPB_FUSNN]] Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
[https://www.uniprot.org/uniprot/ATPA_FUSNN ATPA_FUSNN] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the F1-catalytic domain of the adenosine triphosphate (ATP) synthase has been determined from the pathogenic anaerobic bacterium Fusobacterium nucleatum. The enzyme can hydrolyse ATP but is partially inhibited. The structure is similar to those of the F1-ATPases from Caldalkalibacillus thermarum, which is more strongly inhibited in ATP hydrolysis, and in Mycobacterium smegmatis, which has a very low ATP hydrolytic activity. The betaE-subunits in all three enzymes are in the conventional 'open' state, and in the case of C. thermarum and M. smegmatis, they are occupied by an ADP and phosphate (or sulfate), but in F. nucleatum, the occupancy by ADP appears to be partial. It is likely that the hydrolytic activity of the F. nucleatum enzyme is regulated by the concentration of ADP, as in mitochondria.


Structure of F1-ATPase from the obligate anaerobe Fusobacterium nucleatum.,Petri J, Nakatani Y, Montgomery MG, Ferguson SA, Aragao D, Leslie AGW, Heikal A, Walker JE, Cook GM Open Biol. 2019 Jun 28;9(6):190066. doi: 10.1098/rsob.190066. Epub 2019 Jun 26. PMID:31238823<ref>PMID:31238823</ref>
==See Also==
 
*[[ATPase 3D structures|ATPase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6q45" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Fusobacterium nucleatum subsp. nucleatum ATCC 25586]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aragao, D]]
[[Category: Aragao D]]
[[Category: Cook, G M]]
[[Category: Cook GM]]
[[Category: Ferguson, S A]]
[[Category: Ferguson SA]]
[[Category: Heikal, A]]
[[Category: Heikal A]]
[[Category: Leslie, A G.W]]
[[Category: Leslie AGW]]
[[Category: Montgomery, M G]]
[[Category: Montgomery MG]]
[[Category: Nakatani, Y]]
[[Category: Nakatani Y]]
[[Category: Petri, J]]
[[Category: Petri J]]
[[Category: Walker, J E]]
[[Category: Walker JE]]
[[Category: Atpase]]
[[Category: Complex]]
[[Category: Fusobacterium]]
[[Category: Hydrolase]]

Latest revision as of 07:49, 7 February 2024

F1-ATPase from Fusobacterium nucleatum

6q45, resolution 3.60Å

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