1PY0

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

1PY0 の概要

• エントリーDOI: 10.2210/pdb1py0/pdb
• 分子名称: Pseudoazurin, ZINC ION, YTTRIUM ION, ... (6 entities in total)
• 機能のキーワード: cupredoxin, nmr probe, electron transport
• 由来する生物種: Alcaligenes faecalis
• 細胞内の位置: Periplasm: P04377
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14251.72

構造登録者

Prudencio, M.,Rohovec, J.,Peters, J.A.,Tocheva, E.,Boulanger, M.J.,Murphy, M.E.,Hupkes, H.J.,Kosters, W.,Impagliazzo, A.,Ubbink, M. (登録日: 2003-07-07, 公開日: 2004-12-07, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)