4wo8: Difference between revisions
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''' | ==The substrate -free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni== | ||
<StructureSection load='4wo8' size='340' side='right' caption='[[4wo8]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4wo8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WO8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WO8 FirstGlance]. <br> | |||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Taurocyamine_kinase Taurocyamine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.4 2.7.3.4] </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=4wo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wo8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wo8 RCSB], [http://www.ebi.ac.uk/pdbsum/4wo8 PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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 | 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> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Taurocyamine kinase]] | |||
[[Category: Awama, A]] | |||
[[Category: Gouet, P]] | |||
[[Category: Marcillat, O]] | |||
[[Category: Merceron, R]] | [[Category: Merceron, R]] | ||
[[Category: Montserret, R]] | [[Category: Montserret, R]] | ||
[[Category: | [[Category: Duplicated]] | ||
[[Category: | [[Category: Substrate specificity]] | ||
[[Category: | [[Category: Transferase]] | ||
[[Category: Transition state]] | |||
