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| | <SX load='5fkz' size='340' side='right' viewer='molstar' caption='[[5fkz]], [[Resolution|resolution]] 5.50Å' scene=''> | | <SX load='5fkz' size='340' side='right' viewer='molstar' caption='[[5fkz]], [[Resolution|resolution]] 5.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fkz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FKZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FKZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fkz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FKZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fkx|5fkx]], [[5fl2|5fl2]]</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]] 5.5Å</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=5fkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fkz OCA], [https://pdbe.org/5fkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fkz RCSB], [https://www.ebi.ac.uk/pdbsum/5fkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fkz 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=5fkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fkz OCA], [http://pdbe.org/5fkz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fkz RCSB], [http://www.ebi.ac.uk/pdbsum/5fkz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fkz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DCLZ_ECOLI DCLZ_ECOLI]] LDC is constitutively but weakly expressed under various conditions. | + | [https://www.uniprot.org/uniprot/LDCC_ECOLI LDCC_ECOLI] Plays a role in lysine utilization by acting as a lysine decarboxylase.<ref>PMID:9339543</ref> |
| | <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 K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lysine decarboxylase]]
| + | [[Category: Bacia M]] |
| - | [[Category: Bacia, M]] | + | [[Category: Carriel D]] |
| - | [[Category: Carriel, D]] | + | [[Category: Chan SWS]] |
| - | [[Category: Chan, S W.S]] | + | [[Category: Elsen S]] |
| - | [[Category: Choudens, S Ollagnier de]]
| + | [[Category: Gutsche I]] |
| - | [[Category: Elsen, S]] | + | [[Category: Houry WA]] |
| - | [[Category: Gutsche, I]] | + | [[Category: Kandiah E]] |
| - | [[Category: Houry, W A]] | + | [[Category: Liu K]] |
| - | [[Category: Kandiah, E]] | + | [[Category: Malet H]] |
| - | [[Category: Liu, K]] | + | [[Category: Ollagnier de Choudens S]] |
| - | [[Category: Malet, H]] | + | [[Category: Perard J]] |
| - | [[Category: Perard, J]] | + | |
| - | [[Category: Acid-stress]] | + | |
| - | [[Category: Cage]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Rava]]
| + | |
| Structural highlights
Function
LDCC_ECOLI Plays a role in lysine utilization by acting as a lysine decarboxylase.[1]
Publication Abstract from PubMed
The inducible lysine decarboxylase LdcI is an important enterobacterial acid stress response enzyme whereas LdcC is its close paralogue thought to play mainly a metabolic role. A unique macromolecular cage formed by two decamers of the Escherichia coli LdcI and five hexamers of the AAA+ ATPase RavA was shown to counteract acid stress under starvation. Previously, we proposed a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and crystal structures of an inactive LdcI decamer and a RavA monomer. We now present cryo-electron microscopy 3D reconstructions of the E. coli LdcI and LdcC, and an improved map of the LdcI bound to the LARA domain of RavA, at pH optimal for their enzymatic activity. Comparison with each other and with available structures uncovers differences between LdcI and LdcC explaining why only the acid stress response enzyme is capable of binding RavA. We identify interdomain movements associated with the pH-dependent enzyme activation and with the RavA binding. Multiple sequence alignment coupled to a phylogenetic analysis reveals that certain enterobacteria exert evolutionary pressure on the lysine decarboxylase towards the cage-like assembly with RavA, implying that this complex may have an important function under particular stress conditions.
Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA.,Kandiah E, Carriel D, Perard J, Malet H, Bacia M, Liu K, Chan SW, Houry WA, Ollagnier de Choudens S, Elsen S, Gutsche I Sci Rep. 2016 Apr 15;6:24601. doi: 10.1038/srep24601. PMID:27080013[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamamoto Y, Miwa Y, Miyoshi K, Furuyama J, Ohmori H. The Escherichia coli ldcC gene encodes another lysine decarboxylase, probably a constitutive enzyme. Genes Genet Syst. 1997 Jun;72(3):167-72. PMID:9339543 doi:10.1266/ggs.72.167
- ↑ Kandiah E, Carriel D, Perard J, Malet H, Bacia M, Liu K, Chan SW, Houry WA, Ollagnier de Choudens S, Elsen S, Gutsche I. Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA. Sci Rep. 2016 Apr 15;6:24601. doi: 10.1038/srep24601. PMID:27080013 doi:http://dx.doi.org/10.1038/srep24601
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