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==Crystal Structure of Phosphorylated C.elegans Thymidylate Synthase in Complex with dUMP== | |||
<StructureSection load='4isw' size='340' side='right' caption='[[4isw]], [[Resolution|resolution]] 3.14Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4isw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ISW FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ihi|3ihi]], [[4iqq|4iqq]], [[4irr|4irr]], [[4g9u|4g9u]], [[4iqb|4iqb]], [[4e5o|4e5o]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thymidylate_synthase Thymidylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.45 2.1.1.45] </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=4isw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4isw RCSB], [http://www.ebi.ac.uk/pdbsum/4isw PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
==See Also== | |||
*[[Thymidylate synthase|Thymidylate synthase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caeel]] | |||
[[Category: Thymidylate synthase]] | [[Category: Thymidylate synthase]] | ||
[[Category: Banaszak, K | [[Category: Banaszak, K]] | ||
[[Category: Dowiercial, A | [[Category: Dowiercial, A]] | ||
[[Category: Jarmula, A | [[Category: Jarmula, A]] | ||
[[Category: Rode, W | [[Category: Rode, W]] | ||
[[Category: Rypniewski, W | [[Category: Rypniewski, W]] | ||
[[Category: Wilk, P | [[Category: Wilk, P]] | ||
[[Category: Deoxynucleotide biosynthesis]] | [[Category: Deoxynucleotide biosynthesis]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
Revision as of 19:21, 21 December 2014
Crystal Structure of Phosphorylated C.elegans Thymidylate Synthase in Complex with dUMPCrystal Structure of Phosphorylated C.elegans Thymidylate Synthase in Complex with dUMP
Structural highlights
Publication Abstract from PubMedCrystal 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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