8VQK

YcjN from Escherichia coli

Summary for 8VQK

• Entry DOI: 10.2210/pdb8vqk/pdb
• Descriptor: Putative ABC transporter periplasmic-binding protein YcjN, SULFATE ION, GLYCEROL, ... (7 entities in total)
• Functional Keywords: substrate binding protein, abc transporter cognate binding protein, ligand binding protein, unknown function
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 97451.00

Authors

Trevino, M.A.,Fernandez, D.,Sharaf, N.G. (deposition date: 2024-01-18, release date: 2024-10-09, Last modification date: 2024-11-13)

Primary citation

Trevino, M.A.,Amankwah, K.A.,Fernandez, D.,Weston, S.A.,Stewart, C.J.,Gallardo, J.M.,Shahgholi, M.,Sharaf, N.G.
Expression, purification, and characterization of diacylated Lipo-YcjN from Escherichia coli.
J.Biol.Chem., 300:107853-107853, 2024

PubMed Abstract: YcjN is a putative substrate binding protein expressed from a cluster of genes involved in carbohydrate import and metabolism in Escherichia coli. Here, we determine the crystal structure of YcjN to a resolution of 1.95 Å, revealing that its three-dimensional structure is similar to substrate binding proteins in subcluster D-I, which includes the well-characterized maltose binding protein (MBP). Furthermore, we found that recombinant overexpression of YcjN results in the formation of a lipidated form of YcjN that is posttranslationally diacylated at cysteine 21. Comparisons of size-exclusion chromatography profiles and dynamic light scattering measurements of lipidated and non-lipidated YcjN proteins suggest that lipidated YcjN aggregates in solution via its lipid moiety. Additionally, bioinformatic analysis indicates that YcjN-like proteins may exist in both Bacteria and Archaea, potentially in both lipidated and non-lipidated forms. Together, our results provide a better understanding of the aggregation properties of recombinantly expressed bacterial lipoproteins in solution and establish a foundation for future studies that aim to elucidate the role of these proteins in bacterial physiology.

PubMed: 39362470
DOI: 10.1016/j.jbc.2024.107853

Experimental method

X-RAY DIFFRACTION (1.95 Å)