4U6I

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

Summary for 4U6I

• Entry DOI: 10.2210/pdb4u6i/pdb
• Descriptor: Ethanolamine utilization protein EutL, SODIUM ION, COBALAMIN, ... (4 entities in total)
• Functional Keywords: bacterial microcompartment, eut, bmc shell protein, transport protein, cobalamin, vitamin b12
• Biological source: Clostridium perfringens
• Total number of polymer chains: 3
• Total formula weight: 72503.46

Authors

Thompson, M.C.,Crowley, C.S.,Kopstein, J.S.,Yeates, T.O. (deposition date: 2014-07-29, release date: 2014-10-22, Last modification date: 2023-09-27)

Primary citation

Thompson, M.C.,Crowley, C.S.,Kopstein, J.,Bobik, T.A.,Yeates, T.O.
Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor.
Acta Crystallogr.,Sect.F, 70:1584-1590, 2014

PubMed Abstract: 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 Å 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.

PubMed: 25484204
DOI: 10.1107/S2053230X1402158X

Experimental method

X-RAY DIFFRACTION (2.1 Å)