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5VBA

Structure of EspG1 chaperone from the type VII (ESX-1) secretion system determined with the assistance of N-terminal T4 lysozyme fusion

Summary for 5VBA
Entry DOI10.2210/pdb5vba/pdb
DescriptorLysozyme, ESX-1 secretion-associated protein EspG1 chimera, CHLORIDE ION (3 entities in total)
Functional Keywordsesx-1, type vii secretion system, rv3866, snm5, protein secretion, chaperone, hydrolase
Biological sourceEnterobacteria phage T4
More
Total number of polymer chains2
Total formula weight96353.53
Authors
Korotkov, K.V. (deposition date: 2017-03-29, release date: 2017-07-05, Last modification date: 2023-10-04)
Primary citationTuukkanen, A.T.,Freire, D.,Chan, S.,Arbing, M.A.,Reed, R.W.,Evans, T.J.,Zenkeviciute, G.,Kim, J.,Kahng, S.,Sawaya, M.R.,Chaton, C.T.,Wilmanns, M.,Eisenberg, D.,Parret, A.H.A.,Korotkov, K.V.
Structural Variability of EspG Chaperones from Mycobacterial ESX-1, ESX-3, and ESX-5 Type VII Secretion Systems.
J. Mol. Biol., 431:289-307, 2019
Cited by
PubMed: 30419243
DOI: 10.1016/j.jmb.2018.11.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.27 Å)
Structure validation

218853

건을2024-04-24부터공개중

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