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- PDB-9u8h: Crystal structure of Leminorella grimontii GatC in the absence of... -

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Basic information

Entry
Database: PDB / ID: 9u8h
TitleCrystal structure of Leminorella grimontii GatC in the absence of D-xylose
ComponentsPTS galactitol transporter subunit IIC
KeywordsTRANSPORT PROTEIN / PTS / transporter / xylose
Function / homology
Function and homology information


galactitol transmembrane transporter activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / plasma membrane
Similarity search - Function
Galactitol permease IIC component / Phosphotransferase system, sugar-specific permease component / PTS system sugar-specific permease component / Phosphotransferase system, EIIC component, type 2 / PTS_EIIC type-2 domain profile.
Similarity search - Domain/homology
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate / PTS galactitol transporter subunit IIC
Similarity search - Component
Biological speciesLeminorella grimontii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.74 Å
AuthorsTakahashi, Y.S. / Kohga, H. / Yamamoto, K. / Takahashi, J.F. / Tanaka, Y. / Ichikawa, M. / Miyazaki, R. / Tsukazaki, T.
Funding support Japan, 1items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS) Japan
CitationJournal: FEBS Lett / Year: 2025
Title: Structural basis of a GatC ortholog transporter in the bacterial phosphotransferase system.
Authors: Yutaro S Takahashi / Hidetaka Kohga / Min Fey Chek / Kotomi Yamamoto / Jun F Takahashi / Hideki Shigematsu / Yoshiki Tanaka / Muneyoshi Ichikawa / Ryoji Miyazaki / Toshio Hakoshima / Tomoya Tsukazaki /
Abstract: The bacterial phosphotransferase system (PTS) mediates the uptake of specific carbohydrates via IIC transporters. Here, we report the crystal and cryo-electron microscopy (cryo-EM) structures of ...The bacterial phosphotransferase system (PTS) mediates the uptake of specific carbohydrates via IIC transporters. Here, we report the crystal and cryo-electron microscopy (cryo-EM) structures of Leminorella grimontii galactitol-specific PTS enzyme IIC component (LgGatC), which is implicated in D-xylose uptake and belongs to the ascorbate-galactitol (AG) superfamily of IIC proteins. These structures, determined in the presence and absence of D-xylose, capture the transporter in an outward-facing conformation. A homology model of an inward-facing state, constructed based on these structures, supports an elevator-like transport mechanism. These findings provide structural insights into substrate recognition by GatC and offer a framework for understanding sugar transport in PTS IIC proteins.
History
DepositionMar 26, 2025Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Oct 15, 2025Provider: repository / Type: Initial release
Revision 1.1Mar 4, 2026Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PTS galactitol transporter subunit IIC
B: PTS galactitol transporter subunit IIC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)102,2958
Polymers100,1562
Non-polymers2,1396
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3550 Å2
ΔGint-34 kcal/mol
Surface area35780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)87.870, 100.840, 122.880
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP22121

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Components

#1: Protein PTS galactitol transporter subunit IIC


Mass: 50078.062 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Leminorella grimontii (bacteria) / Gene: SOASR030_34840 / Production host: Escherichia coli (E. coli) / References: UniProt: A0AAV5N9B3
#2: Chemical
ChemComp-OLC / (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate / 1-Oleoyl-R-glycerol


Mass: 356.540 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C21H40O4
Has ligand of interestN
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.72 Å3/Da / Density % sol: 54.74 %
Crystal growTemperature: 293.15 K / Method: lipidic cubic phase / pH: 8
Details: 100 mM Na-acetate, 100 mM Tris-HCl (pH8.0), 40-45% PEG200

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL32XU / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Feb 3, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.74→46.65 Å / Num. obs: 11682 / % possible obs: 99.12 % / Redundancy: 41.6 % / CC1/2: 0.859 / Net I/σ(I): 3.03
Reflection shellResolution: 3.74→3.91 Å / Num. unique obs: 2801 / CC1/2: 0.281

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Processing

Software
NameVersionClassification
PHENIX(1.20.1_4487: ???)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.74→46.65 Å / SU ML: 0.49 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.14 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2855 1167 9.99 %
Rwork0.2536 --
obs0.2568 11682 99.14 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.74→46.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6708 0 104 0 6812
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.004
X-RAY DIFFRACTIONf_angle_d0.635
X-RAY DIFFRACTIONf_dihedral_angle_d6.9641016
X-RAY DIFFRACTIONf_chiral_restr0.0421154
X-RAY DIFFRACTIONf_plane_restr0.0071148
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.74-3.910.34491410.30871268X-RAY DIFFRACTION99
3.91-4.120.33071440.26091308X-RAY DIFFRACTION100
4.12-4.370.25021460.25881302X-RAY DIFFRACTION100
4.37-4.710.41341380.33731246X-RAY DIFFRACTION96
4.71-5.180.27351450.23871319X-RAY DIFFRACTION100
5.19-5.930.29451470.26531327X-RAY DIFFRACTION100
5.93-7.470.26421490.23661332X-RAY DIFFRACTION100
7.47-46.650.19161570.18471413X-RAY DIFFRACTION99

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