View source for 4mld


==X-ray structure of ComE D58E REC domain from Streptococcus pneumoniae==
<StructureSection load='4mld' size='340' side='right'caption='[[4mld]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mld]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MLD FirstGlance]. <br>
</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=4mld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mld OCA], [https://pdbe.org/4mld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mld RCSB], [https://www.ebi.ac.uk/pdbsum/4mld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mld ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8DMW5_STRR6 Q8DMW5_STRR6] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Natural transformation contributes to the maintenance and to the evolution of the bacterial genomes. In Streptococcus pneumoniae, this function is reached by achieving the competence state, which is under the control of the ComD-ComE two-component system. We present the crystal and solution structures of ComE. We mimicked the active and non-active states by using the phosphorylated mimetic ComED58E and the unphosphorylatable ComED58A mutants. In the crystal, full-length ComED58A dimerizes through its canonical REC receiver domain but with an atypical mode, which is also adopted by the isolated RECD58A and RECD58E. The LytTR domain adopts a tandem arrangement consistent with the two direct repeats of its promoters. However ComED58A is monomeric in solution, as seen by SAXS, by contrast to ComED58E that dimerizes. For both, a relative mobility between the two domains is assumed. Based on these results we propose two possible ways for activation of ComE by phosphorylation.

Structural insights into the dimerization of the response regulator ComE from Streptococcus pneumoniae.,Boudes M, Sanchez D, Graille M, van Tilbeurgh H, Durand D, Quevillon-Cheruel S Nucleic Acids Res. 2014 Feb 5. PMID:24500202<ref>PMID:24500202</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mld" style="background-color:#fffaf0;"></div>

==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae R6]]
[[Category: Boudes M]]
[[Category: Durand D]]
[[Category: Graille M]]
[[Category: Quevillon-Cheruel S]]
[[Category: Sanchez D]]
[[Category: Van Tilbeurgh H]]