Literature DB >> 25354690

Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution.

R Sophia Weerth1, Karolina Michalska, Craig A Bingman, Ragothaman M Yennamalli, Hui Li, Robert Jedrzejczak, Fengbin Wang, Gyorgy Babnigg, Andrzej Joachimiak, Michael G Thomas, George N Phillips.   

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.
© 2014 Wiley Periodicals, Inc.

Entities:  

Keywords:  X-ray; cupin; manganese-bound; natural product; structural genomics

Mesh:

Substances:

Year:  2014        PMID: 25354690      PMCID: PMC4300268          DOI: 10.1002/prot.24705

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


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