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5htl
From Proteopedia
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<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=5htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5htl OCA], [http://pdbe.org/5htl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5htl RCSB], [http://www.ebi.ac.uk/pdbsum/5htl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5htl ProSAT]</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=5htl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5htl OCA], [http://pdbe.org/5htl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5htl RCSB], [http://www.ebi.ac.uk/pdbsum/5htl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5htl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | C-di-GMP is a bacterial second messenger regulating various cellular functions. Many bacteria contain c-di-GMP-metabolizing enzymes but lack known c-di-GMP receptors. Recently, two MshE-type ATPases associated with bacterial type II secretion system and type IV pilus formation were shown to specifically bind c-di-GMP. Here we report crystal structure of the MshE N-terminal domain (MshEN1-145) from Vibrio cholerae in complex with c-di-GMP at a 1.37 A resolution. This structure reveals a unique c-di-GMP-binding mode, featuring a tandem array of two highly conserved binding motifs, each comprising a 24-residue sequence RLGxx(L/V/I)(L/V/I)xxG(L/V/I)(L/V/I)xxxxLxxxLxxQ that binds half of the c-di-GMP molecule, primarily through hydrophobic interactions. Mutating these highly conserved residues markedly reduces c-di-GMP binding and biofilm formation by V. cholerae. This c-di-GMP-binding motif is present in diverse bacterial proteins exhibiting binding affinities ranging from 0.5 muM to as low as 14 nM. The MshEN domain contains the longest nucleotide-binding motif reported to date. | ||
| + | |||
| + | Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain.,Wang YC, Chin KH, Tu ZL, He J, Jones CJ, Sanchez DZ, Yildiz FH, Galperin MY, Chou SH Nat Commun. 2016 Aug 31;7:12481. doi: 10.1038/ncomms12481. PMID:27578558<ref>PMID:27578558</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5htl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:07, 19 October 2016
Structure of MshE with cdg
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