Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis for a filamentous morpheein model of human cystathionine beta-synthase.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Jun 6, 2026
Authors	Inayathulla Mohammed / Ela Mijatovic / Thilo Magnus Philipp / Lucia Janickova / Kelly Ascencao / Francisco J Asturias / Luis Alfonso Martinez-Cruz / Csaba Szabo / Henning Stahlberg / Tomas Majtan /
PubMed Abstract	Human cystathionine beta-synthase (CBS) is a vital enzyme that regulates sulfur amino acid metabolism, hydrogen sulfide production, and cellular redox balance. Using a multidisciplinary approach, we ...Human cystathionine beta-synthase (CBS) is a vital enzyme that regulates sulfur amino acid metabolism, hydrogen sulfide production, and cellular redox balance. Using a multidisciplinary approach, we demonstrate that CBS functions as a filamentous morpheein, with its stability, turnover, and activity governed by dynamic quaternary structural transitions. Three distinct filamentous assemblies were resolved by cryo-EM and are mediated by the oligomerization loop (residues 516-525): (i) ligand-free trans-dimers that form trans-basal filaments with basal stability and activity, (ii) adenosylornithine-bound cis-dimers that assemble into stabilized cis-basal filaments and (iii) S-adenosylmethionine-bound allo-dimers, which, together with cis-dimers, form highly stable, allo-activated stacked filaments. These reversible filamentous assemblies redefine CBS biology by integrating oligomerization and allosteric regulation within a morpheein framework. These findings provide a transformative perspective on CBS function and open avenues for pharmacological targeting of dysregulated CBS in various diseases including homocystinuria, cancer, and Down syndrome.
External links	Nat Commun / PubMed:42248820 / PubMed Central
Methods	EM (single particle) / EM (helical sym.)
Resolution	2.0 - 4.11 Å
Structure data	54904 9shm EMDB-54904, PDB-9shm: Structure of trans-basal conformer of human CBS trapped in PLP-aminoacrylate intermediate state (CBS PLP-AA)- by single particle approach Method: EM (single particle) / Resolution: 2.0 Å 54905 9shn EMDB-54905, PDB-9shn: Structure of trans-basal conformer of human CBS trapped in PLP-serine external aldemine intermediate (CBS-PLP-Ser)- by single particle approach Method: EM (single particle) / Resolution: 2.18 Å 54925 9si8 EMDB-54925, PDB-9si8: Structure of trans-basal conformer of human CBS trapped in PLP-aminoacrylate intermediate state (CBS PLP-AA)- by Helical processing. Method: EM (helical sym.) / Resolution: 2.47 Å 55037 9sml EMDB-55037, PDB-9sml: Structure of trans-basal conformer of human CBS trapped in PLP-serine external aldemine intermediate (CBS-PLP-Ser)- by Helical approach Method: EM (helical sym.) / Resolution: 2.78 Å 55097 9spv EMDB-55097, PDB-9spv: focused structure of regulatory domains of cis-basal conformer of human CBS induced by non-activating allosteric SAO ligand - by Helical approach Method: EM (helical sym.) / Resolution: 4.04 Å 55099 9spw EMDB-55099, PDB-9spw: Structure of cis-basal conformer of human CBS induced by non-activating allosteric SAO ligand - by single particle approach. Method: EM (single particle) / Resolution: 4.11 Å 55105 9sq0 EMDB-55105, PDB-9sq0: Structure of trans-basal conformer of wild-type human CBS alone (internal aldemine)- by single particle approach Method: EM (single particle) / Resolution: 2.74 Å 55115 9sqq EMDB-55115, PDB-9sqq: Structure of trans-basal conformer of wild-type human CBS enzyme in absence of substrate and allosteric activators- by Helical approach Method: EM (helical sym.) / Resolution: 3.0 Å
Chemicals	ChemComp-HEM: PROTOPORPHYRIN IX CONTAINING FE ChemComp-P1T: 2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC ACID ChemComp-KOU: (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine ChemComp-SFG: SINEFUNGIN
Source	homo sapiens (human)
Keywords	CYTOSOLIC PROTEIN / transsulfuration pathway / L-serine hydro-lyase / heme-binding protein / CBS domain / LYASE