[English] 日本語
Yorodumi
- PDB-8hjg: Crystal structure of glycosyltransferase SgUGT94-289-3 in complex... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8hjg
TitleCrystal structure of glycosyltransferase SgUGT94-289-3 in complex with M5, state 1
Componentsglycosyltransferase
KeywordsTRANSFERASE / mogroside / UGT / Siraitia grosvenorii
Function / homology: / Chem-POG / URIDINE-5'-DIPHOSPHATE
Function and homology information
Biological speciesSiraitia grosvenorii (monk fruit)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsLi, M. / Zhang, S. / Cui, S.
Funding support China, United Kingdom, 4items
OrganizationGrant numberCountry
Chinese Academy of SciencesXDB27020106 China
National Natural Science Foundation of China (NSFC)U20A2004 China
Chinese Academy of Sciences#YSBR-015 China
CAMS Innovation Fund for Medical Sciences (CIFMS)2021-I2M-1-071 United Kingdom
CitationJournal: Nat Commun / Year: 2024
Title: Structural insights into the catalytic selectivity of glycosyltransferase SgUGT94-289-3 towards mogrosides.
Authors: Cui, S. / Zhang, S. / Wang, N. / Su, X. / Luo, Z. / Ma, X. / Li, M.
History
DepositionNov 23, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 29, 2024Provider: repository / Type: Initial release
Revision 1.1Aug 14, 2024Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _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 / _citation_author.name

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: glycosyltransferase
B: glycosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,61010
Polymers103,1332
Non-polymers4,4778
Water15,871881
1
A: glycosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,8055
Polymers51,5671
Non-polymers2,2384
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area720 Å2
ΔGint-9 kcal/mol
Surface area19170 Å2
MethodPISA
2
B: glycosyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,8055
Polymers51,5671
Non-polymers2,2384
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area740 Å2
ΔGint-8 kcal/mol
Surface area18930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.178, 76.483, 82.182
Angle α, β, γ (deg.)90.000, 92.636, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

-
Components

-
Protein , 1 types, 2 molecules AB

#1: Protein glycosyltransferase


Mass: 51566.711 Da / Num. of mol.: 2 / Mutation: V148G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Siraitia grosvenorii (monk fruit) / Production host: Escherichia coli (E. coli)

-
Non-polymers , 5 types, 889 molecules

#2: Chemical ChemComp-POG / (20S)-2,5,8,11,14,17-HEXAMETHYL-3,6,9,12,15,18-HEXAOXAHENICOSANE-1,20-DIOL / POLYPROPYLENE GLYCOL / HEPTAPROPYLENE GLYCOL


Mass: 424.569 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H44O8
#3: Chemical ChemComp-M1K / (2S,3S,4S,5R,6R)-2-(hydroxymethyl)-6-[[(2R,3S,4S,5R,6R)-6-[[(3S,8S,9R,10R,11R,13R,14S,17R)-17-[(2S,5R)-5-[(2S,3R,4S,5S,6R)-3-[(2R,3R,4S,5S,6S)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-6-[[(2R,3R,4S,5S,6S)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxymethyl]-4,5-bis(oxidanyl)oxan-2-yl]oxy-6-methyl-6-oxidanyl-heptan-2-yl]-4,4,9,13,14-pentamethyl-11-oxidanyl-2,3,7,8,10,11,12,15,16,17-decahydro-1H-cyclopenta[a]phenanthren-3-yl]oxy]-3,4,5-tris(oxidanyl)oxan-2-yl]methoxy]oxane-3,4,5-triol


Mass: 1287.434 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C60H102O29
#4: Chemical ChemComp-UDP / URIDINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 404.161 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H14N2O12P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: UDP*YM
#5: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 881 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.39 Å3/Da / Density % sol: 48.59 %
Crystal growTemperature: 289.15 K / Method: vapor diffusion, hanging drop
Details: Tris-HCl, polyethylene glycol 3350, NaCl, Polypropylene glycol P400.

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97918 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 6, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 1.7→19.65 Å / Num. obs: 102616 / % possible obs: 94.9 % / Redundancy: 6.9 % / Biso Wilson estimate: 18.24 Å2 / CC1/2: 0.999 / Net I/σ(I): 18.36
Reflection shellResolution: 1.7→1.761 Å / Num. unique obs: 10112 / CC1/2: 0.916

-
Processing

Software
NameVersionClassification
Blu-Icedata collection
PHENIX1.18.2_3874refinement
autoPROCdata processing
Aimlessdata scaling
PHENIXphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6JTD

6jtd


Resolution: 1.7→19.65 Å / SU ML: 0.163 / Cross valid method: FREE R-VALUE / σ(F): 1.66 / Phase error: 19.3558
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1906 4863 4.82 %
Rwork0.1796 96030 -
obs0.1801 100891 94.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 23.61 Å2
Refinement stepCycle: LAST / Resolution: 1.7→19.65 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6757 0 286 881 7924
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00987274
X-RAY DIFFRACTIONf_angle_d1.30989912
X-RAY DIFFRACTIONf_chiral_restr0.21081117
X-RAY DIFFRACTIONf_plane_restr0.00631209
X-RAY DIFFRACTIONf_dihedral_angle_d22.71812571
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7-1.720.25321530.24163140X-RAY DIFFRACTION95.98
1.72-1.740.24071710.23423262X-RAY DIFFRACTION96.24
1.74-1.760.26581650.22673204X-RAY DIFFRACTION96.12
1.76-1.780.23241700.22073224X-RAY DIFFRACTION95.61
1.78-1.810.23241510.22423210X-RAY DIFFRACTION96.11
1.81-1.830.26461800.21593217X-RAY DIFFRACTION95.96
1.83-1.860.2191830.21683163X-RAY DIFFRACTION95
1.86-1.890.2361750.22033014X-RAY DIFFRACTION90.67
1.89-1.910.20971730.21233254X-RAY DIFFRACTION96.18
1.91-1.950.20531650.2063225X-RAY DIFFRACTION96.22
1.95-1.980.21731610.2033198X-RAY DIFFRACTION95.86
1.98-2.020.20151750.20383254X-RAY DIFFRACTION96.37
2.02-2.050.21671450.19483245X-RAY DIFFRACTION96.14
2.05-2.10.22061650.19193178X-RAY DIFFRACTION95.51
2.1-2.140.24351370.18863267X-RAY DIFFRACTION95.81
2.14-2.190.18011670.18593205X-RAY DIFFRACTION95.42
2.19-2.250.17611540.18753267X-RAY DIFFRACTION96.07
2.25-2.310.2081310.18453213X-RAY DIFFRACTION95.24
2.31-2.370.19651670.1873116X-RAY DIFFRACTION92.5
2.37-2.450.19261950.1853092X-RAY DIFFRACTION92.75
2.45-2.540.19821720.19573233X-RAY DIFFRACTION96.38
2.54-2.640.20111580.18823267X-RAY DIFFRACTION95.99
2.64-2.760.22641340.18943218X-RAY DIFFRACTION95.53
2.76-2.90.22591420.1893282X-RAY DIFFRACTION95.83
2.9-3.090.17651690.18793225X-RAY DIFFRACTION95.71
3.09-3.320.17681960.17263181X-RAY DIFFRACTION94.57
3.32-3.660.17661470.15993087X-RAY DIFFRACTION90.89
3.66-4.180.14461120.14083305X-RAY DIFFRACTION95.98
4.18-5.250.13421610.13683224X-RAY DIFFRACTION93.92
5.25-19.650.16861890.15863060X-RAY DIFFRACTION88.92

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more