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6I50

Structure of Eiger TNF from S. frugiperda

Summary for 6I50
Entry DOI10.2210/pdb6i50/pdb
DescriptorSFRICE_029225 (2 entities in total)
Functional Keywordstnf, tumour necrosis factor, apoptosis, arthropod, cytokine
Biological sourceSpodoptera frugiperda (Fall armyworm)
Total number of polymer chains1
Total formula weight19034.26
Authors
Bertinelli, M.,Paesen, G.C.,Grimes, J.M.,Renner, M. (deposition date: 2018-11-12, release date: 2019-08-14, Last modification date: 2024-11-06)
Primary citationBertinelli, M.,Paesen, G.C.,Grimes, J.M.,Renner, M.
High-resolution crystal structure of arthropod Eiger TNF suggests a mode of receptor engagement and altered surface charge within endosomes.
Commun Biol, 2:293-293, 2019
Cited by
PubMed Abstract: The tumour necrosis factor alpha (TNFα) superfamily of proteins are critical in numerous biological processes, such as in development and immunity. Eiger is the sole TNFα member described in arthropods such as in the important model organism . To date there are no structural data on any Eiger protein. Here we present the structure of the TNF domain of Eiger from the fall armyworm (SfEiger) to 1.7 Å from a serendipitously obtained crystal without prior knowledge of the protein sequence. Our structure confirms that canonical trimerization is conserved from ancestral TNFs and points towards a mode of receptor engagement. Furthermore, we observe numerous surface histidines on SfEiger, potentially acting as pH switches following internalization into endosomes. Our data contributes to the genome annotation of , a voracious agricultural pest, and can serve as a basis for future structure-function investigations of the TNF system in related arthropods such as .
PubMed: 31396573
DOI: 10.1038/s42003-019-0541-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.69 Å)
Structure validation

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건을2024-11-13부터공개중

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