View source for 4p40


==Chlamydia pneumoniae CopN==
<StructureSection load='4p40' size='340' side='right'caption='[[4p40]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4p40]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_pneumoniae Chlamydia pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P40 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMN:DIMETHYLAMINE'>DMN</scene>, <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4p40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p40 OCA], [https://pdbe.org/4p40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p40 RCSB], [https://www.ebi.ac.uk/pdbsum/4p40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p40 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9Z8L4_CHLPN Q9Z8L4_CHLPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Whereas the actin network is commonly hijacked by pathogens, there are few reports of parasites targeting microtubules. The proposed member of the LcrE protein family from some Chlamydia species, e.g. pCopN from C. pneumoniae, binds tubulin and inhibits microtubule assembly in vitro. From the pCopN structure and its similarity with that of MxiC from Shigella, we definitively confirm CopN as the Chlamydia homolog of the LcrE family of bacterial proteins involved in the regulation of type III secretion. We have also investigated the molecular basis for the pCopN effect on microtubules. We show that pCopN delays microtubule nucleation and acts as a pure tubulin-sequestering protein at steady state. It targets the beta subunit interface involved in the tubulin longitudinal self-association in a way that inhibits nucleotide exchange. pCopN contains three repetitions of a helical motif flanked by disordered N- and C-terminal extensions. We have identified the pCopN minimal tubulin-binding region within the second and third repeats. Together with the intriguing observation that C. trachomatis CopN does not bind tubulin, our data support the notion that, in addition to the shared function of type III secretion regulation, these proteins have evolved different functions in the host cytosol. Our results provide a mechanistic framework for understanding the C. pneumoniae CopN specific inhibition of microtubule assembly.

Biochemical and Structural Insights into Microtubule Perturbation by CopN from Chlamydia pneumoniae.,Nawrotek A, Guimaraes BG, Velours C, Subtil A, Knossow M, Gigant B J Biol Chem. 2014 Jul 23. pii: jbc.M114.568436. PMID:25056950<ref>PMID:25056950</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4p40" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydia pneumoniae]]
[[Category: Large Structures]]
[[Category: Gigant B]]
[[Category: Guimaraes BG]]
[[Category: Knossow M]]
[[Category: Nawrotek A]]