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TitleThe ultra-high affinity transport proteins of ubiquitous marine bacteria.
Journal, issue, pagesNature, Vol. 634, Page 721-728, Year 2024
Publish dateDec 14, 2022 (structure data deposition date)
AuthorsClifton, B.E. / Alcolombri, U. / Uechi, G.I. / Jackson, C.J. / Laurino, P.
External linksNature / PubMed:39261732
MethodsX-ray diffraction
Resolution1.32 - 1.86 Å
Structure data

PDB-8hqq:
Crystal structure of the glucose-binding protein SAR11_0769 from "Candidatus Pelagibacter ubique" HTCC1062 bound to glucose
Method: X-RAY DIFFRACTION / Resolution: 1.86 Å

PDB-8hqr:
Crystal structure of the arginine-/lysine-binding protein SAR11_1210 from 'Candidatus Pelagibacter ubique' HTCC1062 bound to arginine
Method: X-RAY DIFFRACTION / Resolution: 1.32 Å

PDB-8kd0:
Crystal structure of SAR11_0769 from 'Candidatus Pelagibacter ubique' HTCC1062 bound to a co-purified ligand, beta-galactopyranose
Method: X-RAY DIFFRACTION / Resolution: 1.675 Å

PDB-8wch:
Crystal structure of SAR11_0655 bound to a co-purified ligand, L-pyroglutamate
Method: X-RAY DIFFRACTION / Resolution: 1.519 Å

Chemicals

ChemComp-BGC:
beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-ARG:
ARGININE

ChemComp-GAL:
beta-D-galactopyranose

ChemComp-PCA:
PYROGLUTAMIC ACID

ChemComp-NA:
Unknown entry

Source
  • candidatus pelagibacter ubique htcc1062 (bacteria)
KeywordsTRANSPORT PROTEIN / ABC transporter / glucose transporter / periplasmic binding protein / solute-binding protein

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