6q7l: Difference between revisions

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<StructureSection load='6q7l' size='340' side='right'caption='[[6q7l]], [[Resolution|resolution]] 7.60&Aring;' scene=''>
<StructureSection load='6q7l' size='340' side='right'caption='[[6q7l]], [[Resolution|resolution]] 7.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6q7l]] is a 26 chain structure. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q7L FirstGlance]. <br>
<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6Q7L 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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
</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=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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='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='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'>[http://oca.weizmann.ac.il/oca-docs/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>
<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=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>
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== 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]  
[[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]  
<div style="background-color:#fffaf0;">
== 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<ref>PMID:31992852</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6q7l" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lysine decarboxylase]]
[[Category: Lysine decarboxylase]]

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