5h5o: Difference between revisions

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'''Unreleased structure'''


The entry 5h5o is ON HOLD
==A cyclic-GMP-dependent signalling pathway regulates bacterial phytopathogenesis==
<StructureSection load='5h5o' size='340' side='right' caption='[[5h5o]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5h5o]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4kg1 4kg1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H5O FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5h5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h5o OCA], [http://pdbe.org/5h5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h5o RCSB], [http://www.ebi.ac.uk/pdbsum/5h5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h5o ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cyclic guanosine 3',5'-monophosphate (cyclic GMP) is a second messenger whose role in bacterial signalling is poorly understood. A genetic screen in the plant pathogen Xanthomonas campestris (Xcc) identified that XC_0250, which encodes a protein with a class III nucleotidyl cyclase domain, is required for cyclic GMP synthesis. Purified XC_0250 was active in cyclic GMP synthesis in vitro. The linked gene XC_0249 encodes a protein with a cyclic mononucleotide-binding (cNMP) domain and a GGDEF diguanylate cyclase domain. The activity of XC_0249 in cyclic di-GMP synthesis was enhanced by addition of cyclic GMP. The isolated cNMP domain of XC_0249 bound cyclic GMP and a structure-function analysis, directed by determination of the crystal structure of the holo-complex, demonstrated the site of cyclic GMP binding that modulates cyclic di-GMP synthesis. Mutation of either XC_0250 or XC_0249 led to a reduced virulence to plants and reduced biofilm formation in vitro. These findings describe a regulatory pathway in which cyclic GMP regulates virulence and biofilm formation through interaction with a novel effector that directly links cyclic GMP and cyclic di-GMP signalling.


Authors: Chin, K.H., Chou, S.-H.
A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis.,An SQ, Chin KH, Febrer M, McCarthy Y, Yang JG, Liu CL, Swarbreck D, Rogers J, Maxwell Dow J, Chou SH, Ryan RP EMBO J. 2013 Sep 11;32(18):2430-8. doi: 10.1038/emboj.2013.165. Epub 2013 Jul 23. PMID:23881098<ref>PMID:23881098</ref>


Description: A cyclic-GMP-dependent signalling pathway regulates bacterial phytopathogenesis
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Chin, K.H]]
<div class="pdbe-citations 5h5o" style="background-color:#fffaf0;"></div>
[[Category: Chou, S.-H]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chin, K H]]
[[Category: Chou, S H]]
[[Category: Biosynthetic protein]]
[[Category: Cyclic gmp]]
[[Category: Signalling pathway]]
[[Category: Xc0249]]
[[Category: Xc0250]]

Revision as of 16:33, 24 May 2017

A cyclic-GMP-dependent signalling pathway regulates bacterial phytopathogenesisA cyclic-GMP-dependent signalling pathway regulates bacterial phytopathogenesis

Structural highlights

5h5o is a 2 chain structure. This structure supersedes the now removed PDB entry 4kg1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Cyclic guanosine 3',5'-monophosphate (cyclic GMP) is a second messenger whose role in bacterial signalling is poorly understood. A genetic screen in the plant pathogen Xanthomonas campestris (Xcc) identified that XC_0250, which encodes a protein with a class III nucleotidyl cyclase domain, is required for cyclic GMP synthesis. Purified XC_0250 was active in cyclic GMP synthesis in vitro. The linked gene XC_0249 encodes a protein with a cyclic mononucleotide-binding (cNMP) domain and a GGDEF diguanylate cyclase domain. The activity of XC_0249 in cyclic di-GMP synthesis was enhanced by addition of cyclic GMP. The isolated cNMP domain of XC_0249 bound cyclic GMP and a structure-function analysis, directed by determination of the crystal structure of the holo-complex, demonstrated the site of cyclic GMP binding that modulates cyclic di-GMP synthesis. Mutation of either XC_0250 or XC_0249 led to a reduced virulence to plants and reduced biofilm formation in vitro. These findings describe a regulatory pathway in which cyclic GMP regulates virulence and biofilm formation through interaction with a novel effector that directly links cyclic GMP and cyclic di-GMP signalling.

A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis.,An SQ, Chin KH, Febrer M, McCarthy Y, Yang JG, Liu CL, Swarbreck D, Rogers J, Maxwell Dow J, Chou SH, Ryan RP EMBO J. 2013 Sep 11;32(18):2430-8. doi: 10.1038/emboj.2013.165. Epub 2013 Jul 23. PMID:23881098[1]

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

References

  1. An SQ, Chin KH, Febrer M, McCarthy Y, Yang JG, Liu CL, Swarbreck D, Rogers J, Maxwell Dow J, Chou SH, Ryan RP. A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis. EMBO J. 2013 Sep 11;32(18):2430-8. doi: 10.1038/emboj.2013.165. Epub 2013 Jul 23. PMID:23881098 doi:http://dx.doi.org/10.1038/emboj.2013.165

5h5o, resolution 2.12Å

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OCA