4isw

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'''Unreleased structure'''
 
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The entry 4isw is ON HOLD until Paper Publication
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==Crystal Structure of Phosphorylated C.elegans Thymidylate Synthase in Complex with dUMP==
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<StructureSection load='4isw' size='340' side='right'caption='[[4isw]], [[Resolution|resolution]] 3.14&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4isw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ISW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ISW FirstGlance]. <br>
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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]] 3.14&#8491;</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=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</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=4isw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isw OCA], [https://pdbe.org/4isw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4isw RCSB], [https://www.ebi.ac.uk/pdbsum/4isw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4isw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9Y052_CAEEL Q9Y052_CAEEL]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Crystal structure is presented of the binary complex between potassium phosphoramidate-phosphorylated recombinant C. elegans thymidylate synthase and dUMP. On each monomer a single phosphoserine residue (Ser127) was identified, instead of expected phosphohistidine. As 31P NMR studies of both the phosphorylated protein and of potassium phosphoramidate potential to phosphorylate different amino acids point to histidine as the only possible site of the modification, thermodynamically favored intermolecular phosphotransfer from histidine to serine is suggested.
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Authors: Wilk, P., Dowiercial, A., Banaszak, K., Jarmula, A., Rypniewski, W., Rode, W.
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Crystal structure of phosphoramide-phosphorylated thymidylate synthase reveals pSer127, reflecting probably pHis to pSer phosphotransfer.,Wilk P, Jarmula A, Ruman T, Banaszak K, Rypniewski W, Ciesla J, Dowiercial A, Rode W Bioorg Chem. 2013 Nov 21;52C:44-49. doi: 10.1016/j.bioorg.2013.11.003. PMID:24321279<ref>PMID:24321279</ref>
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Description: Crystal Structure of Phosphorylated C.elegans Thymidylate Synthase in Complex with dUMP
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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 4isw" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Caenorhabditis elegans]]
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[[Category: Large Structures]]
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[[Category: Banaszak K]]
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[[Category: Dowiercial A]]
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[[Category: Jarmula A]]
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[[Category: Rode W]]
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[[Category: Rypniewski W]]
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[[Category: Wilk P]]

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Crystal Structure of Phosphorylated C.elegans Thymidylate Synthase in Complex with dUMP

PDB ID 4isw

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