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5xp0

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Current revision (10:19, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5xp0' size='340' side='right'caption='[[5xp0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5xp0' size='340' side='right'caption='[[5xp0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xp0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XP0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XP0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XP0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">csgD, STM1142 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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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=5xp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xp0 OCA], [http://pdbe.org/5xp0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xp0 RCSB], [http://www.ebi.ac.uk/pdbsum/5xp0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xp0 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xp0 OCA], [https://pdbe.org/5xp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xp0 RCSB], [https://www.ebi.ac.uk/pdbsum/5xp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xp0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CSGD_SALTY CSGD_SALTY]] Necessary for transcription of the csgAB operon. May have the capability to respond to starvation and/or high cell density by activating csgBA transcription (By similarity).
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[https://www.uniprot.org/uniprot/CSGD_SALTY CSGD_SALTY] Necessary for transcription of the csgAB operon. May have the capability to respond to starvation and/or high cell density by activating csgBA transcription (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The master regulator CsgD switches planktonic growth to biofilm formation by activating synthesis of curli fimbriae and cellulose in Enterobacteriaceae. CsgD was classified to be the LuxR response regulatory family, while its cognate sensor histidine kinase has not been identified yet. CsgD consists of a C-terminal DNA binding domain and an N-terminal regulatory domain that provokes the upstream signal transduction to further modulate its function. We provide the crystal structure of Salmonella Typhimurium CsgD regulatory domain, which reveals an atypical beta5alpha5 response regulatory receiver domain folding with the alpha2 helix representing as a disorder loop compared to the LuxR/FixJ canonical response regulator, and the structure indicated a noteworthy alpha5 helix similar to the non-canonical master regulator VpsT receiver domain alpha6. CsgD regulatory domain assembles with two dimerization interfaces mainly through alpha1 and alpha5, which has shown similarity to the c-di-GMP independent and stabilized dimerization interface of VpsT from Vibrio cholerae respectively. The potential phosphorylation site D59 is directly involved in the interaction of interfaces I and mutagenesis studies indicated that both dimerization interfaces could be crucial for CsgD activity. The structure reveals important molecular details for the dimerization assembly of CsgD and will shed new insight into its regulation mechanism.
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Crystal structure of master biofilm regulator CsgD regulatory domain reveals an atypical receiver domain.,Wen Y, Ouyang Z, Devreese B, He W, Shao Y, Lu W, Zheng F Protein Sci. 2017 Oct;26(10):2073-2082. doi: 10.1002/pro.3245. Epub 2017 Aug 22. PMID:28758290<ref>PMID:28758290</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5xp0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Salty]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
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[[Category: Ouyang, Z]]
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[[Category: Ouyang Z]]
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[[Category: Wen, Y]]
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[[Category: Wen Y]]
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[[Category: Csgd]]
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[[Category: Phosphorylation]]
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[[Category: Response regulator]]
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[[Category: Signal transduction]]
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[[Category: Transcription]]
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Current revision

Crystal structure of master biofilm regulator CsgD regulatory domain

PDB ID 5xp0

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