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- PDB-2wvk: Mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB... -

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Basic information

Entry
Database: PDB / ID: 2wvk
TitleMannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27 apoprotein
ComponentsMANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE
KeywordsTRANSFERASE / GT-A FOLD
Function / homology
Function and homology information


mannosyl-3-phosphoglycerate synthase activity / mannosylglycerate biosynthetic process / Transferases; Glycosyltransferases; Hexosyltransferases / metal ion binding / cytoplasm
Similarity search - Function
Mannosyl-3-phosphoglycerate synthase / Mannosyl-3-phosphoglycerate synthase (osmo_MPGsynth) / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Nucleotide-diphospho-sugar transferases / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
CITRATE ANION / Mannosyl-3-phosphogylcerate synthase
Similarity search - Component
Biological speciesTHERMUS THERMOPHILUS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.97 Å
AuthorsGoncalves, S. / Borges, N. / Esteves, A.M. / Victor, B. / Soares, C.M. / Santos, H. / Matias, P.M.
Citation
Journal: J.Biol.Chem. / Year: 2010
Title: Structural Analysis of Thermus Thermophilus Hb27 Mannosyl-3-Phosphoglycerate Synthase Provides Evidence for a Second Catalytic Metal Ion and New Insight Into the Retaining Mechanism of Glycosyltransferases.
Authors: Goncalves, S. / Borges, N. / Esteves, A.M. / Victor, B. / Soares, C.M. / Santos, H. / Matias, P.M.
#1: Journal: Acta Crystallogr.,Sect.F / Year: 2009
Title: Crystallization and Preliminary X-Ray Analysis of Mannosyl-3-Phosphoglycerate Synthase from Thermus Thermophilus Hb27
Authors: Goncalves, S. / Borges, N. / Santos, H. / Matias, P.M.
History
DepositionOct 19, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 31, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Feb 19, 2014Group: Database references / Source and taxonomy
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_sheet / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_sheet.number_strands / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE
B: MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,8188
Polymers87,3022
Non-polymers5166
Water1,33374
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4320 Å2
ΔGint-135.5 kcal/mol
Surface area31920 Å2
MethodPISA
Unit cell
Length a, b, c (Å)113.456, 113.456, 195.982
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 6
2114B1 - 6
1216A7 - 8
2216B7 - 8
1314A9 - 30
2314B9 - 30
1416A31 - 39
2416B31 - 39
1514A42
2514B42
1614A43 - 87
2614B43 - 87
1715A88 - 90
2715B88 - 90
1814A91 - 117
2814B91 - 117
1915A118 - 134
2915B118 - 34
11014A135 - 140
21014B135 - 140
11116A141 - 143
21116B141 - 43
11214A144 - 202
21214B144 - 202
11316A203 - 205
21316B203 - 05
11416A209 - 216
21416B209 - 216
11515A217 - 223
21515B217 - 23
11614A224 - 288
21614B224 - 288
11715A289 - 296
21715B289 - 96
11814A293 - 308
21814B293 - 308
11916A309 - 318
21916B309 - 18
12015A319 - 338
22015B319 - 338
12114A339 - 351
22114B339 - 51
12215A352 - 361
22215B352 - 361
12314A362 - 369
22314B362 - 69
12414A370 - 391
22414B370 - 391

NCS oper: (Code: given
Matrix: (0.91947, -0.39203, -0.02981), (-0.39188, -0.91995, 0.01102), (-0.03175, 0.00155, -0.99949)
Vector: -0.88963, -8.07091, 49.83484)

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Components

#1: Protein MANNOSYL-3-PHOSPHOGLYCERATE SYNTHASE /


Mass: 43650.766 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) THERMUS THERMOPHILUS (bacteria) / Strain: HB27 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): ROSETTA
References: UniProt: Q72K30, mannosyl-3-phosphoglycerate synthase
#2: Chemical ChemComp-FLC / CITRATE ANION / Citric acid


Mass: 189.100 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H5O7
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 74 / Source method: isolated from a natural source / Formula: H2O

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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: 3.6 Å3/Da / Density % sol: 65.7 % / Description: NONE
Crystal growpH: 6.5
Details: 0.2 M MAGNESIUM ACETATE, 0.1 M SODIUM CACODYLATE PH 6.5, 30-35% MPD WITH 600 MM ZNCL2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 1.305
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.305 Å / Relative weight: 1
ReflectionResolution: 2.97→45.2 Å / Num. obs: 26864 / % possible obs: 99.4 % / Observed criterion σ(I): 0 / Redundancy: 18.9 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 19.5
Reflection shellResolution: 2.97→3.1 Å / Redundancy: 18.5 % / Rmerge(I) obs: 1.27 / Mean I/σ(I) obs: 2.2 / % possible all: 96.7

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Processing

Software
NameVersionClassification
REFMAC5.5.0088refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2WVL

2wvl


Resolution: 2.97→42.91 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.918 / SU B: 37.486 / SU ML: 0.336 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 1.66 / ESU R Free: 0.396 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
RfactorNum. reflection% reflectionSelection details
Rfree0.26636 1358 5.1 %RANDOM
Rwork0.19779 ---
obs0.20122 25502 99.57 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 71.327 Å2
Baniso -1Baniso -2Baniso -3
1--0.17 Å20 Å20 Å2
2---0.17 Å20 Å2
3---0.33 Å2
Refinement stepCycle: LAST / Resolution: 2.97→42.91 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6076 0 18 74 6168
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0226232
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.7311.9838432
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.6935770
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.46322.767300
X-RAY DIFFRACTIONr_dihedral_angle_3_deg22.474151037
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.3011568
X-RAY DIFFRACTIONr_chiral_restr0.1030.2934
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0214806
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2091.51448
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.3822319
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.1753895
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it1.094.5852
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A2555medium positional0.440.5
2B2555medium positional0.440.5
1A459loose positional0.892.5
2B459loose positional0.892.5
1A2555medium thermal0.882
2B2555medium thermal0.882
1A459loose thermal1.018
2B459loose thermal1.018
LS refinement shellResolution: 2.969→3.046 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.378 81 -
Rwork0.32 1558 -
obs--93.87 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.17791.2920.31255.4706-0.56615.574-0.04660.0949-0.0909-0.15230.12490.93840.6874-0.7366-0.07830.0925-0.0853-0.02410.1351-0.02880.24673.5661-24.992226.374
21.2755-0.04970.46734.4321-1.85485.456-0.22140.01310.28260.38660.18180.4477-1.1095-0.23390.03960.24830.0359-0.0590.0854-0.01740.228111.866814.205523.6606
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 391
2X-RAY DIFFRACTION2B1 - 391

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