[English] 日本語
Yorodumi
- PDB-6htk: X-ray structure of the tryptophan lyase NosL in complex with (R)-... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6htk
TitleX-ray structure of the tryptophan lyase NosL in complex with (R)-(+)-indoline-2-carboxylate
Components3-methyl-2-indolic acid synthase
KeywordsANTIBIOTIC / Radical SAM / FeS cluster / Nosiheptide
Function / homology
Function and homology information


4 iron, 4 sulfur cluster binding / metal ion binding
Similarity search - Function
3-methyl-2-indolic acid synthase / ThiH/NocL/HydG-like / Biotin and Thiamin Synthesis associated domain / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
5'-DEOXYADENOSINE / BROMIDE ION / 1H-indole-2-carboxylic acid / : / METHIONINE / S-ADENOSYL-L-HOMOCYSTEINE / IRON/SULFUR CLUSTER / 3-methyl-2-indolic acid synthase
Similarity search - Component
Biological speciesStreptomyces actuosus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsAmara, P. / Mouesca, J.M. / Bella, M. / Martin, L. / Saragaglia, C. / Gambarelli, S. / Nicolet, Y.
Funding support France, 1items
OrganizationGrant numberCountry
French National Research AgencyANR-16-CE29-0019 France
CitationJournal: J.Am.Chem.Soc. / Year: 2018
Title: Radical S-Adenosyl-l-methionine Tryptophan Lyase (NosL): How the Protein Controls the Carboxyl Radical •CO2-Migration.
Authors: Amara, P. / Mouesca, J.M. / Bella, M. / Martin, L. / Saragaglia, C. / Gambarelli, S. / Nicolet, Y.
History
DepositionOct 4, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 21, 2018Provider: repository / Type: Initial release
Revision 1.1Nov 28, 2018Group: Data collection / Database references / Category: citation / pdbx_database_proc / Item: _citation.title
Revision 1.2Apr 24, 2019Group: Data collection / Database references / Category: citation / pdbx_database_proc
Item: _citation.journal_abbrev / _citation.journal_volume ..._citation.journal_abbrev / _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 24, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_alt_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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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_alt_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.pdbx_ptnr2_label_alt_id / _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.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_symmetry

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 3-methyl-2-indolic acid synthase
B: 3-methyl-2-indolic acid synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,94526
Polymers89,3242
Non-polymers3,62024
Water14,826823
1
A: 3-methyl-2-indolic acid synthase
hetero molecules

A: 3-methyl-2-indolic acid synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,81424
Polymers89,3242
Non-polymers3,48922
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_656-x+1,y,-z+11
Buried area5780 Å2
ΔGint-64 kcal/mol
Surface area26770 Å2
MethodPISA
2
B: 3-methyl-2-indolic acid synthase
hetero molecules

B: 3-methyl-2-indolic acid synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,07628
Polymers89,3242
Non-polymers3,75126
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-x+1,y,-z1
Buried area6650 Å2
ΔGint-64 kcal/mol
Surface area26230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)94.650, 47.010, 114.080
Angle α, β, γ (deg.)90.00, 108.91, 90.00
Int Tables number3
Space group name H-MP121
Components on special symmetry positions
IDModelComponents
11A-756-

HOH

21A-940-

HOH

31A-943-

HOH

41B-795-

HOH

51B-986-

HOH

61B-1016-

HOH

-
Components

-
Protein , 1 types, 2 molecules AB

#1: Protein 3-methyl-2-indolic acid synthase / NosL


Mass: 44662.234 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces actuosus (bacteria) / Gene: nosL, nocL, DMT42_23170
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: C6FX51

-
Non-polymers , 10 types, 847 molecules

#2: Chemical ChemComp-SF4 / IRON/SULFUR CLUSTER / Iron–sulfur cluster


Mass: 351.640 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe4S4
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical
ChemComp-BR / BROMIDE ION / Bromide


Mass: 79.904 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Br
#5: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#6: Chemical ChemComp-SAH / S-ADENOSYL-L-HOMOCYSTEINE / S-Adenosyl-L-homocysteine


Type: L-peptide linking / Mass: 384.411 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C14H20N6O5S
#7: Chemical ChemComp-MET / METHIONINE / Methionine


Type: L-peptide linking / Mass: 149.211 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C5H11NO2S
#8: Chemical ChemComp-5AD / 5'-DEOXYADENOSINE / Deoxyadenosine


Mass: 251.242 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H13N5O3
#9: Chemical ChemComp-ICB / 1H-indole-2-carboxylic acid


Mass: 161.157 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C9H7NO2
#10: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 823 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.62 Å3/Da / Density % sol: 53.12 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop
Details: 14-20% PEG 3350, 0.2 M KBr, 1 mM S-adenosyl-L-methionine (SAM) 15 mg/mL SaNosL (protein buffer: 50 mM Tris pH 8; 150 mM NaCl and 2 mM DTT) 5 equivalents of (R)-(+)-indoline-2-carboxylic acid

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 0.980023 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 24, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.980023 Å / Relative weight: 1
ReflectionResolution: 2→47.109 Å / Num. obs: 124568 / % possible obs: 99.8 % / Redundancy: 5.58 % / Rsym value: 0.098 / Net I/σ(I): 13.18
Reflection shellResolution: 2→2.05 Å / Rsym value: 0.695

-
Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4R34
Resolution: 2→47.109 Å / SU ML: 0.22 / Cross valid method: FREE R-VALUE / σ(F): 1.02 / Phase error: 20.79
RfactorNum. reflection% reflection
Rfree0.1971 6246 5.01 %
Rwork0.1689 --
obs0.1704 124568 99.08 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2→47.109 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5910 0 185 823 6918
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0036355
X-RAY DIFFRACTIONf_angle_d0.6468645
X-RAY DIFFRACTIONf_dihedral_angle_d17.1493807
X-RAY DIFFRACTIONf_chiral_restr0.043943
X-RAY DIFFRACTIONf_plane_restr0.0031135
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.0001-2.02280.33742120.3093914X-RAY DIFFRACTION98
2.0228-2.04660.28392120.26323984X-RAY DIFFRACTION100
2.0466-2.07160.28212070.25923902X-RAY DIFFRACTION99
2.0716-2.09780.26072050.24343905X-RAY DIFFRACTION100
2.0978-2.12540.27622130.22914038X-RAY DIFFRACTION100
2.1254-2.15450.26132140.22884009X-RAY DIFFRACTION100
2.1545-2.18530.23181990.22113851X-RAY DIFFRACTION99
2.1853-2.21790.2172150.2164012X-RAY DIFFRACTION100
2.2179-2.25260.24292080.20713943X-RAY DIFFRACTION99
2.2526-2.28950.2482050.20313954X-RAY DIFFRACTION99
2.2895-2.3290.22782110.19883958X-RAY DIFFRACTION100
2.329-2.37130.24042080.1943987X-RAY DIFFRACTION100
2.3713-2.41690.20952110.18593939X-RAY DIFFRACTION99
2.4169-2.46630.2132160.18234006X-RAY DIFFRACTION99
2.4663-2.51990.25782090.18413947X-RAY DIFFRACTION100
2.5199-2.57850.25162070.18713965X-RAY DIFFRACTION100
2.5785-2.6430.22212090.18083927X-RAY DIFFRACTION99
2.643-2.71440.24822050.17643947X-RAY DIFFRACTION99
2.7144-2.79430.23562110.17443972X-RAY DIFFRACTION99
2.7943-2.88450.20052070.17293881X-RAY DIFFRACTION99
2.8845-2.98750.21842080.16693986X-RAY DIFFRACTION99
2.9875-3.10710.21622080.16323962X-RAY DIFFRACTION99
3.1071-3.24850.17592020.15723895X-RAY DIFFRACTION99
3.2485-3.41970.17712080.14353966X-RAY DIFFRACTION99
3.4197-3.63390.15982090.13743953X-RAY DIFFRACTION99
3.6339-3.91440.15422060.12753874X-RAY DIFFRACTION98
3.9144-4.3080.14742060.12663924X-RAY DIFFRACTION99
4.308-4.93090.12422060.12123906X-RAY DIFFRACTION99
4.9309-6.21010.14792090.14573944X-RAY DIFFRACTION99
6.2101-47.12180.18792000.16833871X-RAY DIFFRACTION97
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
11.1701-0.3827-0.54060.88361.05534.16040.48-0.23680.21180.229-0.1-0.4053-0.54590.8829-0.3250.4803-0.25250.02120.6601-0.08590.469370.133363.245238.9784
21.09970.3649-0.58280.56990.2171.50010.27710.0370.25530.0892-0.03410.0402-0.3027-0.0376-0.18830.41480.04210.09680.25390.05150.198138.456655.298141.4221
31.72930.1463-0.8931.03590.05481.41610.3694-0.10910.3310.1127-0.0467-0.093-0.46860.2233-0.25810.4594-0.03070.11370.2759-0.01560.231848.177160.530640.9107
46.1243-2.27-0.12913.3164-0.37956.80.10010.3253-0.4382-0.1240.11060.15480.3323-0.1584-0.0760.2710.0042-0.01380.2719-0.00320.134443.154643.057427.0889
56.22430.6030.66911.1167-0.05961.47730.0522-0.6199-0.41870.25980.12080.3943-0.0634-0.3997-0.1620.25970.00950.06040.41730.15610.35458.669936.849718.9447
62.30480.2410.02260.7278-0.27120.585-0.06040.0507-0.1813-0.04080.02170.010.0226-0.01930.04370.1126-0.0061-0.0290.168-0.03670.142531.990845.3157-0.0478
72.67990.3637-0.07952.1492-0.06851.5812-0.0847-0.1765-0.50710.25920.04650.03060.1732-0.03940.01760.10040.03-0.00970.18960.03660.227127.920735.91968.4004
82.1773-0.06820.29361.25920.21861.6419-0.0283-0.1897-0.54930.02920.00940.06850.0793-0.06990.0430.1278-0.00210.00050.17720.04790.260924.578135.49848.4337
92.22920.3129-0.02651.0195-0.34851.1542-0.10640.3322-0.1116-0.1370.08720.13840.0273-0.15380.02850.1219-0.0156-0.04810.2107-0.01960.193918.082646.9926-5.6701
104.35421.4124-3.3699.08644.92426.8030.7357-1.7782-0.78340.392-0.5410.12781.2703-1.2649-0.2080.6754-0.3941-0.1490.7213-0.01460.759131.525136.55670.7926
1122222.52042-2.41643.63871.8303-0.12121.5278-0.0242-2.000510.28940.89491.1969-0.17460.39731.16870.10140.928140.596963.742343.4515
125.4651-0.76675.96392.0147-0.08346.80560.02640.05640.0216-0.01410.0051-0.0694-0.0319-0.0813-0.00480.71820.05010.25080.27620.04890.348438.824167.559342.5848
136.5993-4.7836.7353.6317-4.8436.9021-0.06250.0351-0.1088-0.03410.0826-0.0567-0.02-0.07610.02480.1775-0.0037-0.00720.215-0.06150.312832.174232.7295-1.0912
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 15 through 64 )
2X-RAY DIFFRACTION2chain 'A' and (resid 65 through 167 )
3X-RAY DIFFRACTION3chain 'A' and (resid 168 through 365 )
4X-RAY DIFFRACTION4chain 'A' and (resid 366 through 398 )
5X-RAY DIFFRACTION5chain 'B' and (resid 13 through 64 )
6X-RAY DIFFRACTION6chain 'B' and (resid 65 through 190 )
7X-RAY DIFFRACTION7chain 'B' and (resid 191 through 215 )
8X-RAY DIFFRACTION8chain 'B' and (resid 216 through 298 )
9X-RAY DIFFRACTION9chain 'B' and (resid 299 through 393 )
10X-RAY DIFFRACTION10chain 'E' and (resid 501 through 501 )
11X-RAY DIFFRACTION11chain 'D' and (resid 501 through 501 )
12X-RAY DIFFRACTION12chain 'A' and (resid 2460)
13X-RAY DIFFRACTION13chain 'B' and (resid 2460)

+
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