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Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor.

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.

SUBMITTER: Thompson MC

PROVIDER: S-EPMC4259218 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor.

Thompson Michael C MC Crowley Christopher S CS Kopstein Jeffrey J Bobik Thomas A TA Yeates Todd O TO

Acta crystallographica. Section F, Structural biology communications 20141114 Pt 12

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. ...[more]

PMID: 25484204

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