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5wq0

From Proteopedia

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Current revision (09:18, 20 March 2024) (edit) (undo)
 
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<StructureSection load='5wq0' size='340' side='right'caption='[[5wq0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='5wq0' size='340' side='right'caption='[[5wq0]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wq0]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WQ0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wq0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenisporosarcina_sp._TG-14 Paenisporosarcina sp. TG-14]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WQ0 FirstGlance]. <br>
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</td></tr><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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.604&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wq0 OCA], [http://pdbe.org/5wq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wq0 RCSB], [http://www.ebi.ac.uk/pdbsum/5wq0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wq0 ProSAT]</span></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'>[https://proteopedia.org/fgij/fg.htm?mol=5wq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wq0 OCA], [https://pdbe.org/5wq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wq0 RCSB], [https://www.ebi.ac.uk/pdbsum/5wq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wq0 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1W2VN00_9BACL A0A1W2VN00_9BACL]
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The two-component phosphorelay system is the most prevalent mechanism for sensing and transducing environmental signals in bacteria. Spore formation, which relies on the two-component phosphorelay system, enables the longterm survival of the glacial bacterium Paenisporosarcina sp. TG-14 in the extreme cold environment. Spo0A is a key response regulator of the phosphorelay system in the early stage of spore formation. The protein is composed of a regulatory N-terminal phospho-receiver domain and a DNAbinding C-terminal activator domain. We solved the threedimensional structure of the unphosphorylated (inactive) form of the receiver domain of Spo0A (PaSpo0A-R) from Paenisporosarcina sp. TG-14. A structural comparison with phosphorylated (active form) Spo0A from Bacillus stearothermophilus (BsSpo0A) showed minor notable differences. A molecular dynamics study of a model of the active form and the crystal structures revealed significant differences in the alpha4 helix and the preceding loop region where phosphorylation occurs. Although an oligomerization study of PaSpo0A-R by analytical ultracentrifugation (AUC) has shown that the protein is in a monomeric state in solution, both crosslinking and crystal-packing analyses indicate the possibility of weak dimer formation by a previously undocumented mechanism. Collectively, these observations provide insight into the mechanism of phosphorylation-dependent activation unique to Spo0A.
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Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier.,Lee CW, Park SH, Lee SG, Shin SC, Han SJ, Kim HW, Park HH, Kim S, Kim HJ, Park H, Park H, Lee JH J Microbiol. 2017 Mar 9. doi: 10.1007/s12275-017-6599-9. PMID:28281198<ref>PMID:28281198</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 5wq0" 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: Lee, C W]]
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[[Category: Paenisporosarcina sp. TG-14]]
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[[Category: Lee, J H]]
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[[Category: Lee CW]]
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[[Category: Paenisporosarcina sp. tg-14]]
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[[Category: Lee JH]]
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[[Category: Signaling protein]]
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[[Category: Spo0a]]
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Current revision

Receiver domain of Spo0A from Paenisporosarcina sp. TG-14

PDB ID 5wq0

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