4wod: Difference between revisions
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The | ==The duplicated taurocyamine kinase from Schistosoma mansoni complexed with arginine== | ||
<StructureSection load='4wod' size='340' side='right'caption='[[4wod]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wod]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WOD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wod OCA], [https://pdbe.org/4wod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wod RCSB], [https://www.ebi.ac.uk/pdbsum/4wod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wod ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KTRC_SCHMA KTRC_SCHMA] This family of enzymes reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate).<ref>PMID:18765922</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The taurocyamine kinase from the blood fluke Schistosoma mansoni (SmTK) belongs to the phosphagen kinase (PK) family and catalyzes the reversible Mg2+-dependent transfer of a phosphoryl group between ATP and taurocyamine. SmTK is derived from gene duplication, as are all known trematode TKs. Our crystallographic study of SmTK reveals the first atomic structure of both a TK and a PK with a bilobal structure. The two unliganded lobes present a canonical open conformation and interact via their respective C- and N-terminal domains at a helix-mediated interface. This spatial arrangement differs from that observed in true dimeric PKs, in which both N-terminal domains make contact. Our structures of SmTK complexed with taurocyamine or L-arginine compounds explain the mechanism by which an arginine residue of the phosphagen-specificity loop is crucial for substrate specificity. An SmTK crystal was soaked with the dead-end transition-state analog (TSA) components taurocyamine-NO32--MgADP. One SmTK monomer was observed with two bound TSAs and an asymmetric conformation, with the first lobe semi-closed and the second closed. However, isothermal titration calorimetry and enzyme kinetics experiments showed that the two lobes function independently. A small-angle X-ray scattering model of SmTK-TSA in solution with two closed active sites was generated. | |||
The substrate -free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni.,Merceron R, Awama AM, Montserret R, Marcillat O, Gouet P J Biol Chem. 2015 Apr 2. pii: jbc.M114.628909. PMID:25837252<ref>PMID:25837252</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4wod" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Schistosoma mansoni]] | |||
[[Category: Awama A]] | |||
[[Category: Gouet P]] | |||
[[Category: Marcillat O]] | |||
[[Category: Merceron R]] | |||
[[Category: Montserret R]] | |||
