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.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.

Structural highlights 7djq is a 3 chain structure with sequence from Haemophilus influenzae Rd KW20 and Ligilactobacillus salivarius UCC118. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1V9TQZ2_9LACO Publication Abstract from PubMed 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. Moonlighting Biochemistry of Cysteine Synthase: A Species-specific Global Regulator.,Singh RP, Saini N, Sharma G, Rahisuddin R, Patel M, Kaushik A, Kumaran S J Mol Biol. 2021 Nov 5;433(22):167255. doi: 10.1016/j.jmb.2021.167255. Epub 2021 , Sep 20. PMID:34547327 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 7djq, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image