Structural highlights
Publication Abstract from PubMed
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 . (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc.
Crystal structure of the N-terminal domain of EccA ATPase from the ESX-1 secretion system of Mycobacterium tuberculosis.,Wagner JM, Evans TJ, Korotkov KV Proteins. 2013 Jul 2. doi: 10.1002/prot.24351. PMID:23818233[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wagner JM, Evans TJ, Korotkov KV. Crystal structure of the N-terminal domain of EccA ATPase from the ESX-1 secretion system of Mycobacterium tuberculosis. Proteins. 2013 Jul 2. doi: 10.1002/prot.24351. PMID:23818233 doi:10.1002/prot.24351
