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- PDB-1quz: Solution structure of the potassium channel scorpion toxin HSTX1 -

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Basic information

Entry
Database: PDB / ID: 1quz
TitleSolution structure of the potassium channel scorpion toxin HSTX1
ComponentsHSTX1 TOXIN
KeywordsTOXIN / SCORPION TOXIN / ALPHA BETA / MOLECULAR MODELING / POTASSIUM CHANNEL
Function / homologyScorpion short toxins signature. / Scorpion short chain toxin, potassium channel inhibitor / Scorpion short toxin, BmKK2 / Knottin, scorpion toxin-like superfamily / ion channel inhibitor activity / potassium channel regulator activity / toxin activity / extracellular region / Potassium channel toxin alpha-KTx 6.3
Function and homology information
MethodSOLUTION NMR / A COMPLETLY EXTENDED CONFORMATION WAS USED AS THE STARTING STRUCTURE. 25 ITERATIONS WERE MADE. 500 STRUCTURES WERE CALCULATED. RESTRAINED MOLECULAR DYNAMICS AT 600K A SLOW COOLING. MINIMIZATION WERE MADE WITH AN ELECTROSTATIC TERM TOPALLH22X.PRO, PARALLH22X.PRO
AuthorsSavarin, P. / Romi-Lebrun, R. / Zinn-Justin, S. / Lebrun, B. / Nakajima, T. / Gilquin, B. / Menez, A.
Citation
Journal: Protein Sci. / Year: 1999
Title: Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: solution structure of the potassium channel inhibitor HsTX1.
Authors: Savarin, P. / Romi-Lebrun, R. / Zinn-Justin, S. / Lebrun, B. / Nakajima, T. / Gilquin, B. / Menez, A.
#1: Journal: Biochem.J. / Year: 1997
Title: A four-disulfide-bridged toxin, with high affinity towards voltage-gatedc K+ channels, isolated from Heterometrus spinnifer (scorpionidae) venom
Authors: Lebrun, B. / Romi-Lebrun, R. / Martin-Eauclaire, M.F. / Yasuda, A. / Ishiguro, M. / Oyama, Y. / Pongs, O. / Nakajima, T.
#2: Journal: Toxicon / Year: 1998
Title: Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels.
Authors: Rochat, H. / Kharrat, R. / Sabatier, J.M. / Mansuelle, P. / Crest, M. / Martin-Eauclaire, M.F. / Sampieri, F. / Oughideni, R. / Mabrouk, K. / Jacquet, G. / Van Rietschoten, J. / El Ayeb, M.
#3: Journal: Biochemistry / Year: 1997
Title: Purification, characterization, and synthesis of three novel toxins from the Chinese scorpion Buthus martensi, which act on K+ channels
Authors: Romi-Lebrun, R. / Lebrun, B. / Martin-Eauclaire, M.F. / Ishiguro, M. / Escoubas, P. / Wu, F.Q. / Hisada, M. / Pongs, O. / Nakajima, T.
History
DepositionJul 5, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 7, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 13, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HSTX1 TOXIN


Theoretical massNumber of molelcules
Total (without water)3,8351
Polymers3,8351
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 20all calculated structures submitted
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide HSTX1 TOXIN


Mass: 3834.593 Da / Num. of mol.: 1 / Source method: obtained synthetically
Details: SOLID PHASE CHEMICAL SYNTHESIS USING THE FMOC METHODOLOGY. THE SEQUENCE OF THIS PEPTIDE OCCURS NATURALLY IN SCORPIONS (SCORPIONIDAE).
References: UniProt: P59867
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
1222D NOESY
133OFF-RESONANCE ROESY (35)

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Sample preparation

Details
Solution-IDContents
15 MG HSTX1; TSP; HCL FOR PH
25 MG HSTX1; TSP; DCL FOR PD
Sample conditionspH: 4 / Pressure: 1 atm / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Felix97BIOSYMdata analysis
X-PLOR3.1BRUNGERstructure solution
X-PLOR3.1BRUNGERrefinement
RefinementMethod: A COMPLETLY EXTENDED CONFORMATION WAS USED AS THE STARTING STRUCTURE. 25 ITERATIONS WERE MADE. 500 STRUCTURES WERE CALCULATED. RESTRAINED MOLECULAR DYNAMICS AT 600K A SLOW COOLING. ...Method: A COMPLETLY EXTENDED CONFORMATION WAS USED AS THE STARTING STRUCTURE. 25 ITERATIONS WERE MADE. 500 STRUCTURES WERE CALCULATED. RESTRAINED MOLECULAR DYNAMICS AT 600K A SLOW COOLING. MINIMIZATION WERE MADE WITH AN ELECTROSTATIC TERM TOPALLH22X.PRO, PARALLH22X.PRO
Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 20 / Conformers submitted total number: 20

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