4F3V

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

Summary for 4F3V

• Entry DOI: 10.2210/pdb4f3v/pdb
• Descriptor: ESX-1 secretion system protein EccA1, SAMARIUM (III) ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: tetratricopeptide repeat, tpr domain, atpase, protein secretion, protein transport
• Biological source: Mycobacterium tuberculosis
• Cellular location: Cytoplasm (Potential): O69733
• Total number of polymer chains: 2
• Total formula weight: 61625.42

Authors

Korotkov, K.V.,Evans, T.J. (deposition date: 2012-05-09, release date: 2012-06-06, Last modification date: 2024-02-28)

Primary citation

Wagner, J.M.,Evans, T.J.,Korotkov, K.V.
Crystal structure of the N-terminal domain of EccA1 ATPase from the ESX-1 secretion system of Mycobacterium tuberculosis.
Proteins, 82:159-163, 2014

PubMed 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.

PubMed: 23818233
DOI: 10.1002/prot.24351

Experimental method

X-RAY DIFFRACTION (2 Å)