4woe

The duplicated taurocyamine kinase from Schistosoma mansoni with bound transition state analog (TSA) components

spinqualitylabelsall models 4woe, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4woe is a 2 chain structure with sequence from Blood fluke. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3S5, ADP, MG, NO3 Gene: Smp_194770 (Blood fluke) Activity: Taurocyamine kinase, with EC number 2.7.3.4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [KTRC_SCHMA] This family of enzymes reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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