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| | <SX load='6q7l' size='340' side='right' viewer='molstar' caption='[[6q7l]], [[Resolution|resolution]] 7.60Å' scene=''> | | <SX load='6q7l' size='340' side='right' viewer='molstar' caption='[[6q7l]], [[Resolution|resolution]] 7.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6q7l]] is a 26 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q7L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Q7L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6q7l]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q7L FirstGlance]. <br> |
| - | </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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cadA, ldcI, Z5734, ECs5113 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), ravA, yieN, b3746, JW3725 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895]), yieN, ravA, BN17_37001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysine_decarboxylase Lysine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.18 4.1.1.18] </span></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=6q7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q7l OCA], [https://pdbe.org/6q7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q7l RCSB], [https://www.ebi.ac.uk/pdbsum/6q7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q7l 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=6q7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q7l OCA], [http://pdbe.org/6q7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6q7l RCSB], [http://www.ebi.ac.uk/pdbsum/6q7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6q7l ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/J7QAN2_ECOLX J7QAN2_ECOLX]] Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone.[HAMAP-Rule:MF_01625] [[http://www.uniprot.org/uniprot/RAVA_ECOLI RAVA_ECOLI]] Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone.[HAMAP-Rule:MF_01625] | + | [https://www.uniprot.org/uniprot/LDCI_ECOLI LDCI_ECOLI] Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by-products of carbohydrate fermentation. |
| | <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 6q7l" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6q7l" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysine decarboxylase]]
| + | [[Category: Arragain B]] |
| - | [[Category: Arragain, B]] | + | [[Category: Felix J]] |
| - | [[Category: Felix, J]] | + | [[Category: Gutsche I]] |
| - | [[Category: Gutsche, I]] | + | [[Category: Jessop M]] |
| - | [[Category: Jessop, M]] | + | [[Category: Malet H]] |
| - | [[Category: Malet, H]] | + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Moxr atpase]]
| + | |
| Structural highlights
Function
LDCI_ECOLI Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by-products of carbohydrate fermentation.
Publication Abstract from PubMed
The hexameric MoxR AAA+ ATPase RavA and the decameric lysine decarboxylase LdcI form a 3.3 MDa cage, proposed to assist assembly of specific respiratory complexes in E. coli. Here, we show that inside the LdcI-RavA cage, RavA hexamers adopt an asymmetric spiral conformation in which the nucleotide-free seam is constrained to two opposite orientations. Cryo-EM reconstructions of free RavA reveal two co-existing structural states: an asymmetric spiral, and a flat C2-symmetric closed ring characterised by two nucleotide-free seams. The closed ring RavA state bears close structural similarity to the pseudo two-fold symmetric crystal structure of the AAA+ unfoldase ClpX, suggesting a common ATPase mechanism. Based on these structures, and in light of the current knowledge regarding AAA+ ATPases, we propose different scenarios for the ATP hydrolysis cycle of free RavA and the LdcI-RavA cage-like complex, and extend the comparison to other AAA+ ATPases of clade 7.
Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex.,Jessop M, Arragain B, Miras R, Fraudeau A, Huard K, Bacia-Verloop M, Catty P, Felix J, Malet H, Gutsche I Commun Biol. 2020 Jan 28;3(1):46. doi: 10.1038/s42003-020-0772-0. PMID:31992852[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jessop M, Arragain B, Miras R, Fraudeau A, Huard K, Bacia-Verloop M, Catty P, Felix J, Malet H, Gutsche I. Structural insights into ATP hydrolysis by the MoxR ATPase RavA and the LdcI-RavA cage-like complex. Commun Biol. 2020 Jan 28;3(1):46. doi: 10.1038/s42003-020-0772-0. PMID:31992852 doi:http://dx.doi.org/10.1038/s42003-020-0772-0
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