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| | <SX load='4upf' size='340' side='right' viewer='molstar' caption='[[4upf]], [[Resolution|resolution]] 7.50Å' scene=''> | | <SX load='4upf' size='340' side='right' viewer='molstar' caption='[[4upf]], [[Resolution|resolution]] 7.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4upf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_mg1655 Escherichia coli mg1655]. 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://proteopedia.org/fgij/fg.htm?mol=4UPF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4upf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4UPF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4upb|4upb]]</td></tr> | + | </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=4upf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upf OCA], [https://pdbe.org/4upf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4upf RCSB], [https://www.ebi.ac.uk/pdbsum/4upf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4upf ProSAT]</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://proteopedia.org/fgij/fg.htm?mol=4upf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upf OCA], [http://pdbe.org/4upf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4upf RCSB], [http://www.ebi.ac.uk/pdbsum/4upf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4upf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[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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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Escherichia coli mg1655]] | + | [[Category: Escherichia coli str. K-12 substr. MG1655]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysine decarboxylase]]
| + | [[Category: Bacia M]] |
| - | [[Category: Bacia, M]] | + | [[Category: Chan SWS]] |
| - | [[Category: Bakkouri, M El]] | + | [[Category: Effantin G]] |
| - | [[Category: Chan, S W.S]] | + | [[Category: El Bakkouri M]] |
| - | [[Category: Effantin, G]] | + | [[Category: Gutsche I]] |
| - | [[Category: Gutsche, I]] | + | [[Category: Houry WA]] |
| - | [[Category: Houry, W A]] | + | [[Category: Liu K]] |
| - | [[Category: Liu, K]] | + | [[Category: Malet H]] |
| - | [[Category: Malet, H]] | + | |
| - | [[Category: Aaa+ atpase]]
| + | |
| - | [[Category: Acid stress response]]
| + | |
| - | [[Category: Lyase-hydrolase complex]]
| + | |
| 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
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Malet H, Liu K, El Bakkourri M, Chan SW, Effantin G, Bacia M, Houry WA, Gutsche I. Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. Elife. 2014 Aug 5:e03653. doi: 10.7554/eLife.03653. PMID:25097238 doi:http://dx.doi.org/10.7554/eLife.03653
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