5z49: Difference between revisions

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'''Unreleased structure'''


The entry 5z49 is ON HOLD
==Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose-1,5-bisphosphate==
<StructureSection load='5z49' size='340' side='right' caption='[[5z49]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5z49]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z49 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RUB:RIBULOSE-1,5-DIPHOSPHATE'>RUB</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z49 OCA], [http://pdbe.org/5z49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z49 RCSB], [http://www.ebi.ac.uk/pdbsum/5z49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z49 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CMPR_SYNE7 CMPR_SYNE7]] Activates transcription of the cmpABCD operon under carbon dioxide-limited conditions.<ref>PMID:11222586</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The CO2-concentrating mechanism (CCM) has evolved to improve the efficiency of photosynthesis in autotrophic cyanobacteria. CmpR, a LysR-type transcriptional regulator (LTTR) from Synechococcus elongatus PCC 7942, was found to regulate CCM-related genes under low-CO2 conditions. Here, the dimeric structure of the effector-binding domain of CmpR (CmpR-EBD) in complex with the co-activator ribulose 1,5-bisphosphate (RuBP) is reported at 2.15 A resolution. One RuBP molecule binds to the inter-domain cleft between the two subunits of the CmpR-EBD dimer. Structural comparison combined with sequence analyses demonstrated that CmpR-EBD has an overall structure similar to those of LTTRs of known structure, but possesses a distinctly different effector-binding pattern.


Authors: Jiang, Y.L., Didel, M., Sun, H.
Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose 1,5-bisphosphate.,Mahounga DM, Sun H, Jiang YL Acta Crystallogr F Struct Biol Commun. 2018 Aug 1;74(Pt 8):506-511. doi:, 10.1107/S2053230X18008841. Epub 2018 Aug 1. PMID:30084400<ref>PMID:30084400</ref>


Description: Crystal structure of the effector-binding domain of Synechococcus elongatus CmpR in complex with ribulose-1,5-bisphosphate
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Jiang, Y.L]]
<div class="pdbe-citations 5z49" style="background-color:#fffaf0;"></div>
[[Category: Didel, M]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Jiang, Y L]]
[[Category: Mahounga, D M]]
[[Category: Sun, H]]
[[Category: Sun, H]]
[[Category: Cyanobacteria]]
[[Category: Transcription]]
[[Category: Transcription factor]]
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