4u6i

Crystal Structure of the EutL Microcompartment Shell Protein from Clostridium Perfringens Bound to Vitamin B12

spinqualitylabelsall models 4u6i, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4u6i is a 3 chain structure with sequence from "bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: B12, NA Gene: eutL ("Bacillus perfringens" Veillon and Zuber 1898) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The EutL shell protein is a key component of the ethanolamine-utilization microcompartment, which serves to compartmentalize ethanolamine degradation in diverse bacteria. The apparent function of this shell protein is to facilitate the selective diffusion of large cofactor molecules between the cytoplasm and the lumen of the microcompartment. While EutL is implicated in molecular-transport phenomena, the details of its function, including the identity of its transport substrate, remain unknown. Here, the 2.1 A resolution X-ray crystal structure of a EutL shell protein bound to cobalamin (vitamin B12) is presented and the potential relevance of the observed protein-ligand interaction is briefly discussed. This work represents the first structure of a bacterial microcompartment shell protein bound to a potentially relevant cofactor molecule. Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor.,Thompson MC, Crowley CS, Kopstein J, Bobik TA, Yeates TO Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1584-90. doi:, 10.1107/S2053230X1402158X. Epub 2014 Nov 14. PMID:25484204 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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