4Q29

Ensemble Refinement of plu4264 protein from Photorhabdus luminescens

Summary for 4Q29

• Entry DOI: 10.2210/pdb4q29/pdb
• Related: 4MV2
• Descriptor: plu4264 protein, NICKEL (II) ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: structural genomics, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, midwest center for structural genomics, mcsg, cupin, unknown function, psi-biology
• Biological source: Photorhabdus luminescens subsp. laumondii
• Total number of polymer chains: 2
• Total formula weight: 31275.94

Authors

Wang, F.,Michalska, K.,Li, H.,Jedrzejczak, R.,Babnigg, G.,Bingman, C.A.,Yennamalli, R.,Weerth, S.,Miller, M.D.,Thomas, M.G.,Joachimiak, A.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro),Midwest Center for Structural Genomics (MCSG) (deposition date: 2014-04-07, release date: 2014-05-07, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.349 Å)