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Proteins. 2014 Jan;82(1):159-63. doi: 10.1002/prot.24351. Epub 2013 Aug 31.

Crystal structure of the N-terminal domain of EccA₁ ATPase from the ESX-1 secretion system of Mycobacterium tuberculosis.

Author information

1
Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, Kentucky, 40536.

Abstract

EccA1 is an important component of the type VII secretion system (T7SS) that is responsible for transport of virulence factors in pathogenic mycobacteria. EccA1 has an N-terminal domain of unknown function and a C-terminal AAA+ (ATPases associated with various cellular activities) domain. Here we report the crystal structure of the N-terminal domain of EccA1 from Mycobacterium tuberculosis, which shows an arrangement of six tetratricopeptide repeats that may mediate interactions of EccA1 with secreted substrates. Furthermore, the size and shape of the N-terminal domain suggest its orientation in the context of a hexamer model of full-length EccA1.

KEYWORDS:

AAA+ ATPase; Rv3868; TPR domain; tetratricopeptide repeat; type VII secretion system

PMID:
23818233
PMCID:
PMC3927790
DOI:
10.1002/prot.24351
[Indexed for MEDLINE]
Free PMC Article

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