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6zxm
From Proteopedia
(Difference between revisions)
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==Diguanylate cyclase DgcR in complex with c-di-GMP== | ==Diguanylate cyclase DgcR in complex with c-di-GMP== | ||
| - | <StructureSection load='6zxm' size='340' side='right'caption='[[6zxm]]' scene=''> | + | <StructureSection load='6zxm' size='340' side='right'caption='[[6zxm]], [[Resolution|resolution]] 3.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZXM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zxm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Lepbp Lepbp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZXM 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=6zxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zxm OCA], [https://pdbe.org/6zxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zxm RCSB], [https://www.ebi.ac.uk/pdbsum/6zxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zxm ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LEPBI_p0053 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=456481 LEPBP])</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=6zxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zxm OCA], [https://pdbe.org/6zxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zxm RCSB], [https://www.ebi.ac.uk/pdbsum/6zxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zxm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Diguanylate cyclases synthesising the bacterial second messenger c-di-GMP are found to be regulated by a variety of sensory input domains that control the activity of their catalytical GGDEF domain, but how activation proceeds mechanistically is, apart from a few examples, still largely unknown. As part of two-component systems, they are activated by cognate histidine kinases that phosphorylate their Rec input domains. DgcR from Leptospira biflexa is a constitutively dimeric prototype of this class of diguanylate cyclases. Full-length crystal structures reveal that BeF3(-) pseudo-phosphorylation induces a relative rotation of two rigid halves in the Rec domain. This is coupled to a reorganisation of the dimeric structure with concomitant switching of the coiled-coil linker to an alternative heptad register. Finally, the activated register allows the two substrate-loaded GGDEF domains, which are linked to the end of the coiled-coil via a localised hinge, to move into a catalytically competent dimeric arrangement. Bioinformatic analyses suggest that the binary register switch mechanism is utilised by many diguanylate cyclases with N-terminal coiled-coil linkers. | ||
| + | |||
| + | Activation mechanism of a small prototypic Rec-GGDEF diguanylate cyclase.,Teixeira RD, Holzschuh F, Schirmer T Nat Commun. 2021 Apr 12;12(1):2162. doi: 10.1038/s41467-021-22492-7. PMID:33846343<ref>PMID:33846343</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6zxm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Schirmer T]] | + | [[Category: Lepbp]] |
| - | [[Category: Teixeira | + | [[Category: Schirmer, T]] |
| + | [[Category: Teixeira, R D]] | ||
| + | [[Category: C-di-gmp]] | ||
| + | [[Category: Ggdef domain]] | ||
| + | [[Category: Leptospira]] | ||
| + | [[Category: Rec]] | ||
| + | [[Category: Receiver domain]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 10:44, 28 July 2021
Diguanylate cyclase DgcR in complex with c-di-GMP
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