Crystal structure of the N‐terminal domain of EccA 1  ATPase from the ESX‐1 secretion system of  Mycobacterium tuberculosis | Zendy

Wagner Jonathan M. | Zendy; Evans Timothy J. | Zendy; Korotkov Konstantin V. | Zendy

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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.

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