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6TJ4

P. falciparum essential light chain, N-terminal domain

Summary for 6TJ4
Entry DOI10.2210/pdb6tj4/pdb
DescriptorPfELC (2 entities in total)
Functional Keywordsmotility, glideosome, myosin, essential light chain, motor protein
Biological sourcePlasmodium falciparum 3D7
Total number of polymer chains2
Total formula weight18042.41
Authors
Pazicky, S.,Loew, C. (deposition date: 2019-11-25, release date: 2020-10-21, Last modification date: 2024-11-13)
Primary citationPazicky, S.,Dhamotharan, K.,Kaszuba, K.,Mertens, H.D.T.,Gilberger, T.,Svergun, D.,Kosinski, J.,Weininger, U.,Low, C.
Structural role of essential light chains in the apicomplexan glideosome.
Commun Biol, 3:568-568, 2020
Cited by
PubMed Abstract: Gliding, a type of motility based on an actin-myosin motor, is specific to apicomplexan parasites. Myosin A binds two light chains which further interact with glideosome associated proteins and assemble into the glideosome. The role of individual glideosome proteins is unclear due to the lack of structures of larger glideosome assemblies. Here, we investigate the role of essential light chains (ELCs) in Toxoplasma gondii and Plasmodium falciparum and present their crystal structures as part of trimeric sub-complexes. We show that although ELCs bind a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. We suggest that ELCs enhance MyoA performance by inducing secondary structure in MyoA and thus stiffen its lever arm. Structural and biophysical analysis reveals that calcium binding has no influence on the structure of ELCs. Our work represents a further step towards understanding the mechanism of gliding in Apicomplexa.
PubMed: 33051581
DOI: 10.1038/s42003-020-01283-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

231029

數據於2025-02-05公開中

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