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3a5c

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Revision as of 12:16, 29 July 2020

Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase

Structural highlights

3a5c is a 16 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3a5d
Activity:	H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATA_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type alpha chain is a catalytic subunit. [VATD_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. [VATB_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane. The V-type beta chain is a regulatory subunit.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

V-type ATPases (V-ATPases) are categorized as rotary ATP synthase/ATPase complexes. The V-ATPases are distinct from F-ATPases in terms of their rotation scheme, architecture and subunit composition. However, there is no detailed structural information on V-ATPases despite the abundant biochemical and biophysical research. Here, we report a crystallographic study of V1-ATPase, from Thermus thermophilus, which is a soluble component consisting of A, B, D and F subunits. The structure at 4.5 A resolution reveals inter-subunit interactions and nucleotide binding. In particular, the structure of the central stalk composed of D and F subunits was shown to be characteristic of V1-ATPases. Small conformational changes of respective subunits and significant rearrangement of the quaternary structure observed in the three AB pairs were related to the interaction with the straight central stalk. The rotation mechanism is discussed based on a structural comparison between V1-ATPases and F1-ATPases.

Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase.,Numoto N, Hasegawa Y, Takeda K, Miki K EMBO Rep. 2009 Nov;10(11):1228-34. Epub 2009 Sep 25. PMID:19779483^[1]

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

References

↑ Numoto N, Hasegawa Y, Takeda K, Miki K. Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase. EMBO Rep. 2009 Nov;10(11):1228-34. Epub 2009 Sep 25. PMID:19779483 doi:10.1038/embor.2009.202

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3a5c"

@@ Line 1: / Line 1: @@
 ==Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase==
-<StructureSection load='3a5c' size='340' side='right' caption='[[3a5c]], [[Resolution|resolution]] 4.51&Aring;' scene=''>
+<StructureSection load='3a5c' size='340' side='right'caption='[[3a5c]], [[Resolution|resolution]] 4.51&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a5c]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A5C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3a5c]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A5C 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></td></tr>
+</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></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a5d|3a5d]]</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=3a5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5c OCA], [http://pdbe.org/3a5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a5c RCSB], [http://www.ebi.ac.uk/pdbsum/3a5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5c ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3a5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5c OCA], [http://pdbe.org/3a5c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a5c RCSB], [http://www.ebi.ac.uk/pdbsum/3a5c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5c ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[ATPase|ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Thermus thermophilus]]
 [[Category: Hasegawa, Y]]

3a5c

From Proteopedia

Revision as of 12:16, 29 July 2020

Inter-subunit interaction and quaternary rearrangement defined by the central stalk of prokaryotic V1-ATPase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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