Summary for 4MV2
| Entry DOI | 10.2210/pdb4mv2/pdb |
| Descriptor | plu4264, NICKEL (II) ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | structural genomics, psi-biology, midwest center for structural genomics, mcsg, enzyme discovery for natural product biosynthesis, natpro, cupin, unknown function |
| Biological source | Photorhabdus luminescens subsp. laumondii |
| Total number of polymer chains | 2 |
| Total formula weight | 31275.94 |
| Authors | 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) (deposition date: 2013-09-23, release date: 2013-10-02, Last modification date: 2024-10-30) |
| 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 Cited by 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: 25354690DOI: 10.1002/prot.24705 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.349 Å) |
Structure validation
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