4upf: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
''' | ==Assembly principles of the unique cage formed by the ATPase RavA hexamer and the lysine decarboxylase LdcI decamer== | ||
<StructureSection load='4upf' size='340' side='right' caption='[[4upf]], [[Resolution|resolution]] 7.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4upf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UPF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UPF FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4upb|4upb]]</td></tr> | |||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4upf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4upf RCSB], [http://www.ebi.ac.uk/pdbsum/4upf PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A 3.3 MDa macromolecular cage between two E. coli proteins with seemingly incompatible symmetries - the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI - is reconstructed by cryo-electron microscopy to 11 A resolution. Combined with a 7.5 A resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily. | |||
Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.,Malet H, Liu K, El Bakkourri M, Chan SW, Effantin G, Bacia M, Houry WA, Gutsche I Elife. 2014 Aug 5:e03653. doi: 10.7554/eLife.03653. PMID:25097238<ref>PMID:25097238</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lysine decarboxylase]] | |||
[[Category: Bacia, M.]] | |||
[[Category: Bakkouri, M El.]] | |||
[[Category: Chan, S W.S.]] | |||
[[Category: Effantin, G.]] | |||
[[Category: Gutsche, I.]] | |||
[[Category: Houry, W A.]] | |||
[[Category: Liu, K.]] | |||
[[Category: Malet, H.]] | |||
[[Category: Aaa+ atpase]] | |||
[[Category: Acid stress response]] | |||
[[Category: Lyase-hydrolase complex]] | |||
[[Category: Lysine decarboxylase]] | |||
Revision as of 19:25, 20 August 2014
Assembly principles of the unique cage formed by the ATPase RavA hexamer and the lysine decarboxylase LdcI decamerAssembly principles of the unique cage formed by the ATPase RavA hexamer and the lysine decarboxylase LdcI decamer
Structural highlights
Publication Abstract from PubMedA 3.3 MDa macromolecular cage between two E. coli proteins with seemingly incompatible symmetries - the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI - is reconstructed by cryo-electron microscopy to 11 A resolution. Combined with a 7.5 A resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily. Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.,Malet H, Liu K, El Bakkourri M, Chan SW, Effantin G, Bacia M, Houry WA, Gutsche I Elife. 2014 Aug 5:e03653. doi: 10.7554/eLife.03653. PMID:25097238[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||