View source for 5fkz


==Structure of E.coli Constitutive lysine decarboxylase==
<SX load='5fkz' size='340' side='right' viewer='molstar' caption='[[5fkz]], [[Resolution|resolution]] 5.50&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.5&#8491;</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>
</table>
== Function ==
[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;">
== 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<ref>PMID:27080013</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fkz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Bacia M]]
[[Category: Carriel D]]
[[Category: Chan SWS]]
[[Category: Elsen S]]
[[Category: Gutsche I]]
[[Category: Houry WA]]
[[Category: Kandiah E]]
[[Category: Liu K]]
[[Category: Malet H]]
[[Category: Ollagnier de Choudens S]]
[[Category: Perard J]]