5yzv

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==Biophysical and structural characterization of the thermostable WD40 domain of a prokaryotic protein, Thermomonospora curvata PkwA==
==Biophysical and structural characterization of the thermostable WD40 domain of a prokaryotic protein, Thermomonospora curvata PkwA==
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<StructureSection load='5yzv' size='340' side='right' caption='[[5yzv]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='5yzv' size='340' side='right'caption='[[5yzv]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5yzv]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YZV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5yzv]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomonospora_curvata Thermomonospora curvata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YZV FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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]] 2.6&#8491;</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=5yzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzv OCA], [http://pdbe.org/5yzv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yzv RCSB], [http://www.ebi.ac.uk/pdbsum/5yzv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzv 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=5yzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzv OCA], [https://pdbe.org/5yzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yzv RCSB], [https://www.ebi.ac.uk/pdbsum/5yzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PKWA_THECU PKWA_THECU]] May play a regulatory role during the complex growth cycle and in secondary metabolite production.
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[https://www.uniprot.org/uniprot/PKWA_THECU PKWA_THECU] May play a regulatory role during the complex growth cycle and in secondary metabolite production.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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WD40 proteins belong to a big protein family with members identified in every eukaryotic proteome. However, WD40 proteins were only reported in a few prokaryotic proteomes. Using WDSP ( http://wu.scbb.pkusz.edu.cn/wdsp/ ), a prediction tool, we identified thousands of prokaryotic WD40 proteins, among which few proteins have been biochemically characterized. As shown in our previous bioinformatics study, a large proportion of prokaryotic WD40 proteins have higher intramolecular sequence identity among repeats and more hydrogen networks, which may indicate better stability than eukaryotic WD40s. Here we report our biophysical and structural study on the WD40 domain of PkwA from Thermomonospora curvata (referred as tPkwA-C). We demonstrated that the stability of thermophilic tPkwA-C correlated to ionic strength and tPkwA-C exhibited fully reversible unfolding under different denaturing conditions. Therefore, the folding kinetics was also studied through stopped-flow circular dichroism spectra. The crystal structure of tPkwA-C was further resolved and shed light on the key factors that stabilize its beta-propeller structure. Like other WD40 proteins, DHSW tetrad has a significant impact on the stability of tPkwA-C. Considering its unique features, we proposed that tPkwA-C should be a great structural template for protein engineering to study key residues involved in protein-protein interaction of a WD40 protein.
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Biophysical and structural characterization of the thermostable WD40 domain of a prokaryotic protein, Thermomonospora curvata PkwA.,Shen C, Du Y, Qiao F, Kong T, Yuan L, Zhang D, Wu X, Li D, Wu YD Sci Rep. 2018 Aug 28;8(1):12965. doi: 10.1038/s41598-018-31140-y. PMID:30154510<ref>PMID:30154510</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 5yzv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Du, Y]]
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[[Category: Thermomonospora curvata]]
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[[Category: Kong, T]]
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[[Category: Du Y]]
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[[Category: Li, D Y]]
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[[Category: Kong T]]
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[[Category: Qiao, F F]]
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[[Category: Li DY]]
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[[Category: Shen, C]]
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[[Category: Qiao FF]]
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[[Category: Wu, X H]]
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[[Category: Shen C]]
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[[Category: Wu, Y D]]
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[[Category: Wu XH]]
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[[Category: Yuan, L R]]
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[[Category: Wu YD]]
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[[Category: Zhang, D L]]
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[[Category: Yuan LR]]
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[[Category: Prokaryotic]]
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[[Category: Zhang DL]]
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[[Category: Protein binding]]
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[[Category: Reversible folding]]
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[[Category: Thermostable]]
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Current revision

Biophysical and structural characterization of the thermostable WD40 domain of a prokaryotic protein, Thermomonospora curvata PkwA

PDB ID 5yzv

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