1py0
Crystal structure of E51C/E54C Psaz from A.faecalis with CLaNP probe
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OverviewOverview
A lanthanide complex, named CLaNP (caged lanthanide NMR probe) has been, developed for the characterisation of proteins by paramagnetic NMR, spectroscopy. The probe consists of a lanthanide chelated by a derivative, of DTPA (diethylenetriaminepentaacetic acid) with two thiol reactive, functional groups. The CLaNP molecule is attached to a protein by two, engineered, surface-exposed, Cys residues in a bidentate manner. This, drastically limits the dynamics of the metal relative to the protein and, enables measurements of pseudocontact shifts. NMR spectroscopy experiments, on a diamagnetic control and the crystal structure of the probe-protein, complex demonstrate that the protein structure is not affected by probe, attachment. The probe is able to induce pseudocontact shifts to at least, 40 A from the metal and causes residual dipolar couplings due to alignment, at a high magnetic field. The molecule exists in several isomeric forms, with different paramagnetic tensors; this provides a fast way to obtain, long-range distance restraints.
About this StructureAbout this Structure
1PY0 is a Single protein structure of sequence from Alcaligenes faecalis with ZN, Y1, SO4 and YMA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
A caged lanthanide complex as a paramagnetic shift agent for protein NMR., Prudencio M, Rohovec J, Peters JA, Tocheva E, Boulanger MJ, Murphy ME, Hupkes HJ, Kosters W, Impagliazzo A, Ubbink M, Chemistry. 2004 Jul 5;10(13):3252-60. PMID:15224334
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