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. 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 nonlipidated 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 nonlipidated 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)