7njv: Difference between revisions
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==Mycobacterium smegmatis ATP synthase Fo combined class 2== | |||
<StructureSection load='7njv' size='340' side='right'caption='[[7njv]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7njv]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NJV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BQ1:BEDAQUILINE'>BQ1</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=7njv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7njv OCA], [https://pdbe.org/7njv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7njv RCSB], [https://www.ebi.ac.uk/pdbsum/7njv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7njv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ATPF_MYCS2 ATPF_MYCS2] 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_01398] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).[HAMAP-Rule:MF_01398] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from Mycobacterium smegmatis This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360 degrees catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an alpha-subunit in a loop in the gamma-subunit, as proposed before, but also a "fail-safe" mechanism involving the b'-subunit in the peripheral stalk that enhances engagement. A third unreported characteristic is that the fused bdelta-subunit contains a duplicated domain in its N-terminal region where the two copies of the domain participate in similar modes of attachment of the two of three N-terminal regions of the alpha-subunits. The auto-inhibitory plus the associated "fail-safe" mechanisms and the modes of attachment of the alpha-subunits provide targets for development of innovative antitubercular drugs. The structure also provides support for an observation made in the bovine ATP synthase that the transmembrane proton-motive force that provides the energy to drive the rotary mechanism is delivered directly and tangentially to the rotor via a Grotthuss water chain in a polar L-shaped tunnel. | |||
Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis.,Montgomery MG, Petri J, Spikes TE, Walker JE Proc Natl Acad Sci U S A. 2021 Nov 23;118(47):e2111899118. doi: , 10.1073/pnas.2111899118. PMID:34782468<ref>PMID:34782468</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Montgomery | <div class="pdbe-citations 7njv" style="background-color:#fffaf0;"></div> | ||
[[Category: Petri | |||
[[Category: | ==See Also== | ||
[[Category: | *[[ATPase 3D structures|ATPase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycolicibacterium smegmatis MC2 155]] | |||
[[Category: Montgomery MG]] | |||
[[Category: Petri J]] | |||
[[Category: Spikes TE]] | |||
[[Category: Walker JE]] | |||
Latest revision as of 11:56, 14 July 2024
Mycobacterium smegmatis ATP synthase Fo combined class 2Mycobacterium smegmatis ATP synthase Fo combined class 2
Structural highlights
FunctionATPF_MYCS2 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_01398] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).[HAMAP-Rule:MF_01398] Publication Abstract from PubMedThe structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from Mycobacterium smegmatis This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360 degrees catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an alpha-subunit in a loop in the gamma-subunit, as proposed before, but also a "fail-safe" mechanism involving the b'-subunit in the peripheral stalk that enhances engagement. A third unreported characteristic is that the fused bdelta-subunit contains a duplicated domain in its N-terminal region where the two copies of the domain participate in similar modes of attachment of the two of three N-terminal regions of the alpha-subunits. The auto-inhibitory plus the associated "fail-safe" mechanisms and the modes of attachment of the alpha-subunits provide targets for development of innovative antitubercular drugs. The structure also provides support for an observation made in the bovine ATP synthase that the transmembrane proton-motive force that provides the energy to drive the rotary mechanism is delivered directly and tangentially to the rotor via a Grotthuss water chain in a polar L-shaped tunnel. Structure of the ATP synthase from Mycobacterium smegmatis provides targets for treating tuberculosis.,Montgomery MG, Petri J, Spikes TE, Walker JE Proc Natl Acad Sci U S A. 2021 Nov 23;118(47):e2111899118. doi: , 10.1073/pnas.2111899118. PMID:34782468[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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