4mv2 › Citations

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

Weerth RS, Michalska K, Bingman CA, Yennamalli RM, Li H, Jedrzejczak R, Wang F, Babnigg G, Joachimiak A, Thomas MG, Phillips GN
Proteins 83 383-8 (2015)
Cited: 3 times
EuropePMC logo PMID: 25354690

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.

Articles - 4mv2 mentioned but not cited (1)

  1. Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 Å resolution. Weerth RS, Michalska K, Bingman CA, Yennamalli RM, Li H, Jedrzejczak R, Wang F, Babnigg G, Joachimiak A, Thomas MG, Phillips GN. Proteins 83 383-388 (2015)


Reviews citing this publication (2)

  1. Identifying and Visualizing Macromolecular Flexibility in Structural Biology. Palamini M, Canciani A, Forneris F. Front Mol Biosci 3 47 (2016)
  2. Integrating Experiment and Theory to Understand TCR-pMHC Dynamics. Buckle AM, Borg NA. Front Immunol 9 2898 (2018)


Quick links