Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution
| Autor: | Michael G. Thomas, Gyorgy Babnigg, George N. Phillips, Karolina Michalska, Robert Jedrzejczak, Craig A. Bingman, Ragothaman M. Yennamalli, R. Sophia Weerth, Hui Li, Andrzej Joachimiak, Fengbin Wang |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Manganese Binding Sites Resolution (mass spectrometry) biology Crystallography X-Ray biology.organism_classification Ligand (biochemistry) Biochemistry Article Protein Structure Secondary Structural genomics Bacterial Proteins Structural Biology Photorhabdus luminescens Binding site Photorhabdus Molecular Biology Function (biology) Bacteria |
| Zdroj: | Proteins: Structure, Function, and Bioinformatics. 83:1003-1003 |
| ISSN: | 0887-3585 |
| DOI: | 10.1002/prot.24798 |
| Popis: | Proteins belonging to the cupin superfamily have a wide range of catalytic and non-catalytic 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text