4q29 | pdb_00004q29

Ensemble Refinement of plu4264 protein from Photorhabdus luminescens

spinqualitylabelsall models 4q29, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q29 is a 2 chain structure with sequence from Photorhabdus laumondii subsp. laumondii TTO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.349Å, 20 models Ligands: MSE, NA, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A and identified manganese as the likely natural metal ligand of the protein. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc. Structure of a cupin protein Plu4264 from Photorhabdus luminescens subsp. laumondii TTO1 at 1.35 A resolution.,Weerth RS, Michalska K, Bingman CA, Yennamalli RM, Li H, Jedrzejczak R, Wang F, Babnigg G, Joachimiak A, Thomas MG, Phillips GN Proteins. 2014 Oct 30. doi: 10.1002/prot.24705. PMID:25354690 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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