5bn4: Difference between revisions
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==Structure of a unique ATP synthase NeqA-NeqB in complex with ANP from Nanoarcheaum equitans== | ==Structure of a unique ATP synthase NeqA-NeqB in complex with ANP from Nanoarcheaum equitans== | ||
<StructureSection load='5bn4' size='340' side='right' caption='[[5bn4]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='5bn4' size='340' side='right'caption='[[5bn4]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bn4]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5bn4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nanoarchaeum_equitans_Kin4-M Nanoarchaeum equitans Kin4-M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BN4 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=5bn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bn4 OCA], [https://pdbe.org/5bn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bn4 RCSB], [https://www.ebi.ac.uk/pdbsum/5bn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bn4 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/VATA_NANEQ VATA_NANEQ] Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5bn4" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5bn4" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chichili | [[Category: Nanoarchaeum equitans Kin4-M]] | ||
[[Category: Jobichen | [[Category: Chichili VPR]] | ||
[[Category: Mohanty | [[Category: Jobichen C]] | ||
[[Category: Sivaraman | [[Category: Mohanty S]] | ||
[[Category: Sivaraman J]] | |||
Revision as of 09:00, 7 June 2023
Structure of a unique ATP synthase NeqA-NeqB in complex with ANP from Nanoarcheaum equitansStructure of a unique ATP synthase NeqA-NeqB in complex with ANP from Nanoarcheaum equitans
Structural highlights
FunctionVATA_NANEQ Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit. Publication Abstract from PubMedATP synthesis is a critical and universal life process carried out by ATP synthases. Whereas eukaryotic and prokaryotic ATP synthases are well characterized, archaeal ATP synthases are relatively poorly understood. The hyperthermophilic archaeal parasite, Nanoarcheaum equitans lacks several subunits of the ATP synthase and is suspected to be energetically dependent on its host, Ignicoccus hospitalis. This suggests that this ATP synthase might be a rudimentary machine. Here, we report the crystal structure and biophysical studies of the regulatory subunit, NeqB, the apo NeqAB, and NeqAB in complex with nucleotides, ADP and AMP-PNP. NeqB is approximately 20 amino acids shorter at its C-terminus than its homologs but this does not impede its binding with NeqA to form the complex. The heterodimeric NeqAB complex assumes a closed, rigid conformation irrespective of nucleotide binding; this differs from its homologs, which require conformational changes for catalytic activity. Thus, although N. equitans possesses an ATP synthase core A3B3 hexameric complex, it might not function as a bona fide ATP synthase. Structural basis for a unique ATP synthase core complex from Nanoarcheaum Equitans.,Mohanty S, Jobichen C, Chichili VP, Velazquez-Campoy A, Low BC, Hogue CW, Sivaraman J J Biol Chem. 2015 Sep 14. pii: jbc.M115.677492. PMID:26370083[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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