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 DOI | 10.2210/pdb5vba/pdb |
Descriptor | Lysozyme, ESX-1 secretion-associated protein EspG1 chimera, CHLORIDE ION (3 entities in total) |
Functional Keywords | esx-1, type vii secretion system, rv3866, snm5, protein secretion, chaperone, hydrolase |
Biological source | Enterobacteria phage T4 More |
Total number of polymer chains | 2 |
Total formula weight | 96353.53 |
Authors | Korotkov, K.V. (deposition date: 2017-03-29, release date: 2017-07-05, Last modification date: 2023-10-04) |
Primary citation | Tuukkanen, 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: 30419243DOI: 10.1016/j.jmb.2018.11.003 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.27 Å) |
Structure validation
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