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- EMDB-19587: CryoEM structure of M. smegmatis GMP reductase in complex with GM... -

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Basic information

Entry
Database: EMDB / ID: EMD-19587
TitleCryoEM structure of M. smegmatis GMP reductase in complex with GMP and ATP at pH 6.6, compressed conformation.
Map dataLoc-Scale filtered
Sample
  • Complex: Msm GMPR with GMP and ATP at pH 6.6
    • Protein or peptide: GMP reductase
  • Ligand: GUANOSINE-5'-MONOPHOSPHATE
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: water
KeywordsGMP reductase / GuaB1 / CBS domain / Mycobacterium smegmatis / OXIDOREDUCTASE
Function / homology
Function and homology information


GMP reductase / GMP reductase activity / IMP salvage / IMP dehydrogenase activity / purine ribonucleoside salvage / cytosol
Similarity search - Function
GMP reductase-like / : / Inosine-5'-monophosphate dehydrogenase / IMP dehydrogenase/GMP reductase / IMP dehydrogenase / GMP reductase domain / IMP dehydrogenase / GMP reductase domain / CBS domain superfamily / CBS domain / CBS domain / CBS domain profile. / Aldolase-type TIM barrel
Similarity search - Domain/homology
Biological speciesMycolicibacterium smegmatis (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.48 Å
AuthorsDolezal M / Kouba T / Pichova I
Funding supportEuropean Union, 1 items
OrganizationGrant numberCountry
European Union (EU)LX22NPO5103European Union
CitationJournal: Nat Commun / Year: 2026
Title: Structural basis for allosteric regulation of mycobacterial guanosine 5´-monophosphate reductase by ATP and GTP.
Authors: Michal Doležal / Zdeněk Knejzlík / Tomáš Kouba / Anatolij Filimoněnko / Hana Šváchová / Matteo Dedola / Martin Klíma / Iva Pichová /
Abstract: Guanosine 5'-monophosphate reductase (GMPR) is a crucial enzyme in the purine salvage pathway that catalyses the NADPH-dependent conversion of GMP to IMP, thereby contributing to purine nucleotide ...Guanosine 5'-monophosphate reductase (GMPR) is a crucial enzyme in the purine salvage pathway that catalyses the NADPH-dependent conversion of GMP to IMP, thereby contributing to purine nucleotide homeostasis. Mycobacterium smegmatis GMPR (MsmGMPR) contains a regulatory cystathionine β-synthase (CBS) domain, which mediates allosteric modulation by ATP and GTP. However, MsmGMPR exhibits an atypical tertiary structure that is incompatible with the acknowledged regulatory mechanisms of IMPDH/GMPR family enzymes. Here, we combine X-ray crystallography, cryogenic electron microscopy, and biochemical binding assays to elucidate the molecular basis of MsmGMPR regulation by ATP and GTP. We show that ATP stabilises a compressed conformation that inhibits the enzyme by restricting access to the active site and preventing NADPH binding. In contrast, GTP counteracts ATP binding, promoting an active conformation that enables catalysis. Our results provide insight into how MsmGMPR senses and responds to the purine nucleotide balance, revealing a distinct utilisation of the CBS domain compared with its typical role in IMPDH/GMPR enzymes.
History
DepositionFeb 8, 2024-
Header (metadata) releaseAug 20, 2025-
Map releaseAug 20, 2025-
UpdateApr 22, 2026-
Current statusApr 22, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_19587.png

Downloads & links

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Map

FileDownload / File: emd_19587.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationLoc-Scale filtered
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 440 pix.
= 366.784 Å		0.83 Å/pix.
x 440 pix.
= 366.784 Å		0.83 Å/pix.
x 440 pix.
= 366.784 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.8336 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.12
Minimum - Maximum-0.21668342 - 0.8834822
Average (Standard dev.)0.0018900178 (±0.020903403)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 366.784 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_19587_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: RELION post-processed and masked

Fileemd_19587_additional_1.map
AnnotationRELION post-processed and masked
Projections & Slices
AxesZYX

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Histogram

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Half map: #2

Fileemd_19587_half_map_1.map
Projections & Slices
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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_19587_half_map_2.map
Projections & Slices
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Histogram

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Sample components

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Entire : Msm GMPR with GMP and ATP at pH 6.6

EntireName: Msm GMPR with GMP and ATP at pH 6.6
Components
  • Complex: Msm GMPR with GMP and ATP at pH 6.6
    • Protein or peptide: GMP reductase
  • Ligand: GUANOSINE-5'-MONOPHOSPHATE
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: water

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Supramolecule #1: Msm GMPR with GMP and ATP at pH 6.6

SupramoleculeName: Msm GMPR with GMP and ATP at pH 6.6 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Mycolicibacterium smegmatis (bacteria) / Strain: ATCC 700084 / mc(2)155

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Macromolecule #1: GMP reductase

MacromoleculeName: GMP reductase / type: protein_or_peptide / ID: 1 / Details: Guanosine 5'-monophosphate reductase / Number of copies: 8 / Enantiomer: LEVO / EC number: GMP reductase
Source (natural)Organism: Mycolicibacterium smegmatis (bacteria) / Strain: ATCC 700084 / mc(2)155
Molecular weightTheoretical: 51.782434 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MVRFLDGHTP AYDLTYNDVF VVPGRSDVAS RFDVDLSTVD GSGTTIPVVV ANMTAVAGRR MAETVARRGG IVVLPQDLPI TAVSETVDF VKSRDLVVDT PVTLSPEDSV SDANALLHKR AHGAAVVVFE GRPIGLVTEA NCAGVDRFAR VRDIALSDFV T APVGTDPR ...String:
MVRFLDGHTP AYDLTYNDVF VVPGRSDVAS RFDVDLSTVD GSGTTIPVVV ANMTAVAGRR MAETVARRGG IVVLPQDLPI TAVSETVDF VKSRDLVVDT PVTLSPEDSV SDANALLHKR AHGAAVVVFE GRPIGLVTEA NCAGVDRFAR VRDIALSDFV T APVGTDPR EVFDLLEHAP IDVAVMTAPD GTLAGVLTRT GAIRAGIYTP AVDAKGRLRI AAAVGINGDV GAKAQALAEA GA DLLVIDT AHGHQAKMLD AIKAVASLDL GLPLVAGNVV SAEGTRDLIE AGASIVKVGV GPGAMCTTRM MTGVGRPQFS AVV ECAAAA RQLGGHVWAD GGVRHPRDVA LALAAGASNV MIGSWFAGTY ESPGDLLFDR DDRPYKESYG MASKRAVAAR TAGD SSFDR ARKGLFEEGI STSRMSLDPA RGGVEDLLDH ITSGVRSTCT YVGAANLPEL HEKVVLGVQS AAGFAEGHPL PAGWT AAAK EDLEHHHHHH HH

UniProtKB: GMP reductase

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Macromolecule #2: GUANOSINE-5'-MONOPHOSPHATE

MacromoleculeName: GUANOSINE-5'-MONOPHOSPHATE / type: ligand / ID: 2 / Number of copies: 8 / Formula: 5GP
Molecular weightTheoretical: 363.221 Da
Chemical component information

ChemComp-5GP:
GUANOSINE-5'-MONOPHOSPHATE

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Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 8 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #4: water

MacromoleculeName: water / type: ligand / ID: 4 / Number of copies: 214 / Formula: HOH
Molecular weightTheoretical: 18.015 Da
Chemical component information

ChemComp-HOH:
WATER

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 6.6
Component:
ConcentrationFormulaName
50.0 mMHEPES2-[4-(2-Hydroxyethyl)piperazin-1-yl]ethane-1-sulfonic acid
100.0 mMKClPotassium chloride
2.0 mMMgCl2Magnesium chloride
VitrificationCryogen name: ETHANE
Details20 mg/ml Msm GMPR with 2 mM GMP and 5 mM ATP in the storage buffer (50 mM Tris, pH 8.0, 2.5 mM TCEP) was diluted with the cryoEM buffer (50 mM HEPES, pH 6.6, 100 mM KCl, 2 mM MgCl2).

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average exposure time: 2.0 sec. / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 30.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.9 µm
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING ONLY
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

7r50

Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.48 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 107511
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0)
FSC plot (resolution estimation)

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Atomic model buiding 1

DetailsThe initial structure was obtained by fitting an appropriate model into the cryo-EM map using MolRep and ChimeraX. The structure was then refined by iterative manual rebuilding in Coot and Isolde, and automatic refinement in phenix.real_space_refine.
RefinementSpace: REAL
Output model

PDB-8ry5:
CryoEM structure of M. smegmatis GMP reductase in complex with GMP and ATP at pH 6.6, compressed conformation.

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