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4u0m

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Revision as of 01:17, 19 January 2017

Structure of the Vibrio cholerae di-nucleotide cyclase (DncV) mutant D193N in complex with ATP, GTP and 5MTHFGLU2

Structural highlights

4u0m is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	4u03, 4u0l, 4u0n
Activity:	Cyclic GMP-AMP synthase, with EC number 2.7.7.86
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DNCV_VIBCH] Catalyzes the synthesis of cyclic AMP-GMP from ATP and GTP. Is also able to produce c-di-AMP and c-di-GMP from ATP and GTP, respectively; however, c-AMP-GMP is the dominant molecule produced by DncV in vivo. Is required for efficient V.cholerae intestinal colonization, and down-regulates the colonization-influencing process of chemotaxis. Is not active with dATP, TTP, UTP, and CTP.

Publication Abstract from PubMed

Cyclic dinucleotides are a newly expanded class of second messengers that contribute to the regulation of multiple different pathways in bacterial, eukaryotic, and archaeal cells. The recently identified Vibrio cholerae dinucleotide cyclase (DncV, the gene product of VC0179) can generate three different cyclic dinucleotides and preferentially synthesize a hybrid cyclic-GMP-AMP. Here, we report the crystal structural and functional studies of DncV. We unexpectedly observed a 5-methyltetrahydrofolate diglutamate (5MTHFGLU2) molecule bound in a surface pocket opposite the nucleotide substrate-binding groove of DncV. Subsequent mutagenesis and functional studies showed that the enzymatic activity of DncV is regulated by folate-like molecules, suggesting the existence of a signaling pathway that links folate-like metabolism cofactors to the regulation of cyclic dinucleotide second messenger synthesis. Sequence analysis showed that the residues involved in 5MTHFGLU2 binding are highly conserved in DncV orthologs, implying the presence of this regulation mechanism in a wide variety of bacteria.

Structural Biochemistry of a Vibrio cholerae Dinucleotide Cyclase Reveals Cyclase Activity Regulation by Folates.,Zhu D, Wang L, Shang G, Liu X, Zhu J, Lu D, Wang L, Kan B, Zhang JR, Xiang Y Mol Cell. 2014 Sep 18;55(6):931-7. doi: 10.1016/j.molcel.2014.08.001. Epub 2014, Sep 4. PMID:25201413^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhu D, Wang L, Shang G, Liu X, Zhu J, Lu D, Wang L, Kan B, Zhang JR, Xiang Y. Structural Biochemistry of a Vibrio cholerae Dinucleotide Cyclase Reveals Cyclase Activity Regulation by Folates. Mol Cell. 2014 Sep 18;55(6):931-7. doi: 10.1016/j.molcel.2014.08.001. Epub 2014, Sep 4. PMID:25201413 doi:http://dx.doi.org/10.1016/j.molcel.2014.08.001

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4u0m"

@@ Line 1: / Line 1: @@
 ==Structure of the Vibrio cholerae di-nucleotide cyclase (DncV) mutant D193N in complex with ATP, GTP and 5MTHFGLU2==
 <StructureSection load='4u0m' size='340' side='right' caption='[[4u0m]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u03|4u03]], [[4u0l|4u0l]], [[4u0n|4u0n]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclic_GMP-AMP_synthase Cyclic GMP-AMP synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.86 2.7.7.86] </span></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=4u0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4u0m RCSB], [http://www.ebi.ac.uk/pdbsum/4u0m PDBsum]</span></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=4u0m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u0m OCA], [http://pdbe.org/4u0m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u0m RCSB], [http://www.ebi.ac.uk/pdbsum/4u0m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u0m ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4u0m" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cyclic GMP-AMP synthase|Cyclic GMP-AMP synthase]]
 == References ==
 <references/>

4u0m

From Proteopedia

Revision as of 01:17, 19 January 2017

Structure of the Vibrio cholerae di-nucleotide cyclase (DncV) mutant D193N in complex with ATP, GTP and 5MTHFGLU2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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