View source for 5cet


==Crystal structure of Rv2837c==
<StructureSection load='5cet' size='340' side='right' caption='[[5cet]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cet]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CET FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ceu|5ceu]]</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=5cet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cet OCA], [http://pdbe.org/5cet PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cet RCSB], [http://www.ebi.ac.uk/pdbsum/5cet PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/NRNA_MYCTU NRNA_MYCTU]] Bifunctional enzyme which has both oligoribonuclease and pAp-phosphatase activities. Degrades RNA oligonucleotides with a length of 5 nucleotides and shorter, with a preference for 2-mers. Also degrades 24-mers. Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP.<ref>PMID:22114320</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The intracellular infections of Mycobacterium tuberculosis, which is the causative agent of tuberculosis, are regulated by many cyclic dinucleotide signaling. Rv2837c from M. tuberculosis is a soluble, stand-alone DHH-DHHA1 domain phosphodiesterase that down-regulates c-di-AMP through catalytic degradation and plays an important role in M. tuberculosis infections. Here, we report the crystal structure of Rv2837c (2.0 A), and its complex with hydrolysis intermediate 5'-pApA (2.35 A). Our structures indicate that both DHH and DHHA1 domains are essential for c-di-AMP degradation. Further structural analysis shows that Rv2837c does not distinguish adenine from guanine, which explains why Rv2837c hydrolyzes all linear dinucleotides with almost the same efficiency. We observed that Rv2837c degraded other c-di-NMPs at a lower rate than it did on c-di-AMP. Nevertheless, our data also showed that Rv2837c significantly decreases concentrations of both c-di-AMP and c-di-GMP in vivo. Our results suggest that beside its major role in c-di-AMP degradation Rv2837c could also regulate c-di-GMP signaling pathways in bacterial cell.

Structural and Biochemical Insight into the Mechanism of Rv2837c from Mycobacterium tuberculosis as a c-di-NMP Phosphodiesterase.,He Q, Wang F, Liu S, Zhu D, Cong H, Gao F, Li B, Wang H, Lin Z, Liao J, Gu L J Biol Chem. 2016 Feb 12;291(7):3668-81. doi: 10.1074/jbc.M115.699801. Epub 2015 , Dec 14. PMID:26668313<ref>PMID:26668313</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cet" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gu, L]]
[[Category: He, Q]]
[[Category: Liu, S]]
[[Category: Wang, F]]
[[Category: Zhu, D]]
[[Category: C-di-amp]]
[[Category: Hydrolase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Phosphodiesterase]]