4woe: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==The substrate -free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni==

== Structural highlights ==

<table><tr><td colspan='2'>[[4woe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WOE FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3S5:TAUROCYAMINE'>3S5</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=4woe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4woe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4woe RCSB], [http://www.ebi.ac.uk/pdbsum/4woe 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>

== 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 ~~entry 4woe is ON HOLD until Paper Publication~~

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>

~~Authors: Merceron~~, R., Awama, A~~., Montserret, R., Marcillat, O.,~~ Gouet, P.

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~Description: The substrate -free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni~~

== References ==

[[Category: ~~Unreleased Structures~~]]

__TOC__

</StructureSection>

[[Category: Taurocyamine kinase]]

[[Category: Awama, A]]

[[Category: Gouet, P]]

[[Category: Marcillat, O]]

[[Category: Merceron, R]]

[[Category: Montserret, R]]

[[Category: ~~Awama, A~~]]

[[Category: Duplicated]]

[[Category: ~~Marcillat, O~~]]

[[Category: Substrate specificity]]

[[Category: ~~Gouet, P~~]]

[[Category: Transferase]]

[[Category: Transition state]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==The substrate -free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni==
+<StructureSection load='4woe' size='340' side='right' caption='[[4woe]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4woe]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WOE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WOE FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3S5:TAUROCYAMINE'>3S5</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=4woe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4woe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4woe RCSB], [http://www.ebi.ac.uk/pdbsum/4woe 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 entry 4woe is ON HOLD  until Paper Publication
+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>
-Authors: Merceron, R., Awama, A., Montserret, R., Marcillat, O., Gouet, P.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: The substrate -free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Taurocyamine kinase]]
+[[Category: Awama, A]]
+[[Category: Gouet, P]]
+[[Category: Marcillat, O]]
 [[Category: Merceron, R]]
 [[Category: Montserret, R]]
-[[Category: Awama, A]]
+[[Category: Duplicated]]
-[[Category: Marcillat, O]]
+[[Category: Substrate specificity]]
-[[Category: Gouet, P]]
+[[Category: Transferase]]
+[[Category: Transition state]]