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


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.

SUBMITTER: Weerth RS 

PROVIDER: S-EPMC4300268 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature

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

Weerth R Sophia RS   Michalska Karolina K   Bingman Craig A CA   Yennamalli Ragothaman M RM   Li Hui H   Jedrzejczak Robert R   Wang Fengbin F   Babnigg Gyorgy G   Joachimiak Andrzej A   Thomas Michael G MG   Phillips George N GN  

Proteins 20141218 2


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  ...[more]

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