7ZAL

FNIP family proteins from Cafeteria roenbergensis virus (CroV): leucine-rich repeats with novel structural features

This is a non-PDB format compatible entry.

Summary for 7ZAL

• Entry DOI: 10.2210/pdb7zal/pdb
• Related: 6NYR 6NYS
• Descriptor: Crov539 (2 entities in total)
• Functional Keywords: fnip ip22 lrr, unknown function
• Biological source: Cafeteria roenbergensis virus
• Total number of polymer chains: 6
• Total formula weight: 204522.21

Authors

Huyton, T.,Goerlich, D. (deposition date: 2022-03-22, release date: 2022-08-24, Last modification date: 2024-05-01)

Primary citation

Huyton, T.,Jaiswal, M.,Taxer, W.,Fischer, M.,Gorlich, D.
Crystal structures of FNIP/FGxxFN motif-containing leucine-rich repeat proteins.
Sci Rep, 12:16430-16430, 2022

PubMed Abstract: The Cafeteria roenbergensis virus (Crov), Dictyostelium, and other species encode a large family of leucine-rich repeat (LRR) proteins with FGxxFN motifs. We determined the structures of two of them and observed several unique structural features that set them aside from previously characterized LRR family members. Crov588 comprises 25 regular repeats with a LxxLxFGxxFNQxIxENVLPxx consensus, forming a unique closed circular repeat structure. Novel features include a repositioning of a conserved asparagine at the middle of the repeat, a double phenylalanine spine that generates an alternate core packing arrangement, and a histidine/tyrosine ladder on the concave surface. Crov539 is smaller, comprising 12 repeats of a similar LxxLxFGxxFNQPIExVxW/LPxx consensus and forming an unusual cap-swapped dimer structure. The phenylalanine spine of Crov539 is supplemented with a tryptophan spine, while a hydrophobic isoleucine-rich patch is found on the central concave surface. We present a detailed analysis of the structures of Crov588 and Crov539 and compare them to related repeat proteins and other LRR classes.

PubMed: 36180492
DOI: 10.1038/s41598-022-20758-8

Experimental method

X-RAY DIFFRACTION (2.732 Å)