4MV2

Crystal structure of plu4264 protein from Photorhabdus luminescens

「4I4A」から置き換えられました

4MV2 の概要

• エントリーDOI: 10.2210/pdb4mv2/pdb
• 分子名称: plu4264, NICKEL (II) ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: structural genomics, psi-biology, midwest center for structural genomics, mcsg, enzyme discovery for natural product biosynthesis, natpro, cupin, unknown function
• 由来する生物種: Photorhabdus luminescens subsp. laumondii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31275.94

構造登録者

Michalska, K.,Li, H.,Jedrzejczak, R.,Babnigg, G.,Bingman, C.A.,Yennamalli, R.,Weerth, S.,Thomas, M.G.,Phillips Jr., G.N.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG),Enzyme Discovery for Natural Product Biosynthesis (NatPro) (登録日: 2013-09-23, 公開日: 2013-10-02, 最終更新日: 2024-10-30)

主引用文献

Weerth, R.S.,Michalska, K.,Bingman, C.A.,Yennamalli, R.M.,Li, H.,Jedrzejczak, R.,Wang, F.,Babnigg, G.,Joachimiak, A.,Thomas, M.G.,Phillips, G.N.
Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 angstrom resolution.
Proteins, 83:383-388, 2015

PubMed Abstract: Proteins belonging to the cupin superfamily have a wide range of catalytic and noncatalytic functions. Cupin proteins commonly have the capacity to bind a metal ion with the metal frequently determining the function of the protein. We have been investigating the function of homologous cupin proteins that are conserved in more than 40 species of bacteria. To gain insights into the potential function of these proteins we have solved the structure of Plu4264 from Photorhabdus luminescens TTO1 at a resolution of 1.35 Å and identified manganese as the likely natural metal ligand of the protein.

PubMed: 25354690
DOI: 10.1002/prot.24705

実験手法

X-RAY DIFFRACTION (1.349 Å)