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Crystal structure of the N‐terminal domain of EccA 1 ATPase from the ESX‐1 secretion system of Mycobacterium tuberculosis
Author(s) -
Wagner Jonathan M.,
Evans Timothy J.,
Korotkov Konstantin V.
Publication year - 2014
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24351
Subject(s) - tetratricopeptide , random hexamer , secretion , context (archaeology) , mycobacterium tuberculosis , domain (mathematical analysis) , virulence , microbiology and biotechnology , atpase , terminal (telecommunication) , biology , chemistry , biochemistry , tuberculosis , gene , enzyme , engineering , medicine , paleontology , mathematical analysis , telecommunications , mathematics , pathology
EccA 1 is an important component of the type VII secretion system (T7SS) that is responsible for transport of virulence factors in pathogenic mycobacteria. EccA 1 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 EccA 1 from Mycobacterium tuberculosis, which shows an arrangement of six tetratricopeptide repeats that may mediate interactions of EccA 1 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 EccA 1 . Proteins 2014; 82:159–163. © 2013 Wiley Periodicals, Inc.