7DJQ

Crystal Structure of O-acetyl L-serine sulfhydrylase from Haemophilus influenzae in complex with C-Terminal peptide of ribosomal S4 Domain protein from Lactobacillus salivarius.

Summary for 7DJQ

• Entry DOI: 10.2210/pdb7djq/pdb
• Descriptor: C-Terminal peptide of ribosomal S4 Domain protein, Cysteine synthase, SODIUM ION, ... (4 entities in total)
• Functional Keywords: complex, enzyme, inhibitor, transferase
• Biological source: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd); More
• Total number of polymer chains: 3
• Total formula weight: 75746.10

Authors

Saini, N.,Rahisuddin, R.,Kumaran, S. (deposition date: 2020-11-20, release date: 2020-12-09, Last modification date: 2023-11-29)

Primary citation

Singh, R.P.,Saini, N.,Sharma, G.,Rahisuddin, R.,Patel, M.,Kaushik, A.,Kumaran, S.
Moonlighting Biochemistry of Cysteine Synthase: A Species-specific Global Regulator.
J.Mol.Biol., 433:167255-167255, 2021

PubMed Abstract: Cysteine Synthase (CS), the enzyme that synthesizes cysteine, performs non-canonical regulatory roles by binding and modulating functions of disparate proteins. Beyond its role in catalysis and regulation in the cysteine biosynthesis pathway, it exerts its moonlighting effect by binding to few other proteins which possess a C-terminal "CS-binding motif", ending with a terminal ILE. Therefore, we hypothesized that CS might regulate many other disparate proteins with the "CS-binding motif". In this study, we developed an iterative sequence matching method for mapping moonlighting biochemistry of CS and validated our prediction by analytical and structural approaches. Using a minimal protein-peptide interaction system, we show that five previously unknown CS-binder proteins that participate in diverse metabolic processes interact with CS in a species-specific manner. Furthermore, results show that signatures of protein-protein interactions, including thermodynamic, competitive-inhibition, and structural features, highly match the known CS-Binder, serine acetyltransferase (SAT). Together, the results presented in this study allow us to map the extreme multifunctional space (EMS) of CS and reveal the biochemistry of moonlighting space, a subset of EMS. We believe that the integrated computational and experimental workflow developed here could be further modified and extended to study protein-specific moonlighting properties of multifunctional proteins.

PubMed: 34547327
DOI: 10.1016/j.jmb.2021.167255

Experimental method

X-RAY DIFFRACTION (2.3 Å)