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	Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 5226, Year 2022
Publish date	Sep 5, 2022
Authors	Nicholas Spellmon / Artur Muszyński / Ireneusz Górniak / Jiri Vlach / David Hahn / Parastoo Azadi / Jochen Zimmer /
PubMed Abstract	O antigens are ubiquitous protective extensions of lipopolysaccharides in the extracellular leaflet of the Gram-negative outer membrane. Following biosynthesis in the cytosol, the lipid-linked ...O antigens are ubiquitous protective extensions of lipopolysaccharides in the extracellular leaflet of the Gram-negative outer membrane. Following biosynthesis in the cytosol, the lipid-linked polysaccharide is transported to the periplasm by the WzmWzt ABC transporter. Often, O antigen secretion requires the chemical modification of its elongating terminus, which the transporter recognizes via a carbohydrate-binding domain (CBD). Here, using components from A. aeolicus, we identify the O antigen structure with methylated mannose or rhamnose as its cap. Crystal and cryo electron microscopy structures reveal how WzmWzt recognizes this cap between its carbohydrate and nucleotide-binding domains in a nucleotide-free state. ATP binding induces drastic conformational changes of its CBD, terminating interactions with the O antigen. ATPase assays and site directed mutagenesis reveal reduced hydrolytic activity upon O antigen binding, likely to facilitate polymer loading into the ABC transporter. Our results elucidate critical steps in the recognition and translocation of polysaccharides by ABC transporters.
External links	Nat Commun / PubMed:36064941 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.61 - 4.1 Å
Structure data	27491 8dku EMDB-27491, PDB-8dku: CryoEM structure of the A. aeolicus WzmWzt transporter bound to the native O antigen Method: EM (single particle) / Resolution: 3.2 Å 27494 8dl0 EMDB-27494, PDB-8dl0: CryoEM structure of the nucleotide-free and open channel A.aeolicus WzmWzt transporter Method: EM (single particle) / Resolution: 4.1 Å 27556 8dn8 EMDB-27556, PDB-8dn8: CryoEM structure of the A. aeolicus WzmWzt transporter bound to 3-O-methyl-D-mannose Method: EM (single particle) / Resolution: 3.7 Å 27563 8dnc EMDB-27563, PDB-8dnc: CryoEM structure of the A. aeolicus WzmWzt transporter bound to the native O antigen and ADP Method: EM (single particle) / Resolution: 3.3 Å 27564 8dne EMDB-27564, PDB-8dne: CryoEM structure of the A.aeolicus WzmWzt transporter bound to ATP Method: EM (single particle) / Resolution: 3.5 Å 27623 8dou EMDB-27623, PDB-8dou: CryoEM structure of the A. aeolicus WzmWzt transporter bound to ADP Method: EM (single particle) / Resolution: 3.54 Å PDB-8dky: Crystal structure of the Aquifex aeolicus Wzt Carbohydrate Binding Domain bound to 3-O-methyl-D-mannose Method: X-RAY DIFFRACTION / Resolution: 1.61 Å
Chemicals	ChemComp-U90: 3-O-methyl-alpha-D-mannopyranose ChemComp-HOH: WATER / Water ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate
Source	aquifex aeolicus (bacteria) aquifex aeolicus vf5 (bacteria)
Keywords	TRANSLOCASE / O antigen / ABC transporter / CBD-dependent / SUGAR BINDING PROTEIN / O antigen ABC transporter / carbohydrate binding domain / 3-O-methyl-D-mannose