5Y70

NMR structure of KMP11 in DPC micelle

Summary for 5Y70

• Entry DOI: 10.2210/pdb5y70/pdb
• NMR Information: BMRB: 36112
• Descriptor: Kinetoplastid membrane protein 11 (1 entity in total)
• Functional Keywords: dpc micelle, kinetoplastid membrane protein-11, trypanosomes, membrane protein
• Biological source: Trypanosoma brucei brucei
• Cellular location: Cytoplasm, cytoskeleton : P69300
• Total number of polymer chains: 1
• Total formula weight: 12071.57

Authors

Lu, Y.,Lim, L.Z.,Song, J. (deposition date: 2017-08-16, release date: 2018-02-07, Last modification date: 2024-05-15)

Primary citation

Lim, L.Z.,Ee, S.,Fu, J.,Tan, Y.,He, C.Y.,Song, J.
Kinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle.
FEBS Lett., 591:3793-3804, 2017

PubMed Abstract: Kinetoplastid membrane protein-11 (KMP11) is a membrane-associated surface protein of kinetoplastids, which has a strong antigenicity but no mammalian homolog, thus representing a promising vaccine candidate. Here, by CD and NMR, we revealed that in buffer, KMP11 assumes a highly helical conformation without stable tertiary packing. Remarkably, upon interacting with dodecylphosphocholine (DPC) micelle, despite minor changes in secondary structures, KMP11 undergoes rearrangements to form a defined structure. We found that its three-dimensional structure unexpectedly adopts the classic four-helix bundle fold. The surface constituted by the N-/C-termini and conserved loop was characterized to dynamically interact with the polar phase of DPC micelle. Our results provide a structural basis for understanding KMP11 functions and further offer a promising avenue for engineering better vaccines.

PubMed: 29082514
DOI: 10.1002/1873-3468.12891

Experimental method

SOLUTION NMR