1PY0

Crystal structure of E51C/E54C Psaz from A.faecalis with CLaNP probe

Summary for 1PY0

• Entry DOI: 10.2210/pdb1py0/pdb
• Descriptor: Pseudoazurin, ZINC ION, YTTRIUM ION, ... (6 entities in total)
• Functional Keywords: cupredoxin, nmr probe, electron transport
• Biological source: Alcaligenes faecalis
• Cellular location: Periplasm: P04377
• Total number of polymer chains: 1
• Total formula weight: 14251.72

Authors

Prudencio, M.,Rohovec, J.,Peters, J.A.,Tocheva, E.,Boulanger, M.J.,Murphy, M.E.,Hupkes, H.J.,Kosters, W.,Impagliazzo, A.,Ubbink, M. (deposition date: 2003-07-07, release date: 2004-12-07, Last modification date: 2024-10-30)

Primary citation

Prudencio, M.,Rohovec, J.,Peters, J.A.,Tocheva, E.,Boulanger, M.J.,Murphy, M.E.,Hupkes, H.J.,Kosters, W.,Impagliazzo, A.,Ubbink, M.
A caged lanthanide complex as a paramagnetic shift agent for protein NMR.
Chemistry, 10:3252-3260, 2004

PubMed Abstract: 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.

PubMed: 15224334
DOI: 10.1002/chem.200306019

Experimental method

X-RAY DIFFRACTION (2 Å)