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- PDB-2lvw: Solution NMR studies of the dimeric regulatory subunit IlvN of th... -

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Basic information

Entry
Database: PDB / ID: 2lvw
TitleSolution NMR studies of the dimeric regulatory subunit IlvN of the E.coli Acetohydroxyacid synthase I (AHAS I)
ComponentsAcetolactate synthase isozyme 1 small subunit
KeywordsTRANSFERASE / AHAS / Regulatory subunit / ACT domain / IlvN / Valine / Branched chain amino acid biosynthesis
Function / homology
Function and homology information


acetolactate synthase regulator activity / acetolactate synthase complex / acetolactate synthase / branched-chain amino acid biosynthetic process / acetolactate synthase activity / L-valine biosynthetic process / isoleucine biosynthetic process / cytosol
Similarity search - Function
Acetolactate synthase, small subunit / AHAS, ACT domain / AHAS-like ACT domain / ACT domain / ACT domain / ACT domain profile. / ACT domain / ACT-like domain / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Acetolactate synthase isozyme 1 small subunit
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model1
AuthorsKaranth, M.N. / Sarma, S.P.
CitationJournal: Biochemistry / Year: 2013
Title: The coil-to-helix transition in IlvN regulates the allosteric control of Escherichia coli acetohydroxyacid synthase I
Authors: Karanth, N.M. / Sarma, S.P.
History
DepositionJul 12, 2012Deposition site: BMRB / Processing site: PDBJ
Revision 1.0May 29, 2013Provider: repository / Type: Initial release
Revision 1.1May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Acetolactate synthase isozyme 1 small subunit
B: Acetolactate synthase isozyme 1 small subunit


Theoretical massNumber of molelcules
Total (without water)22,5262
Polymers22,5262
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 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Acetolactate synthase isozyme 1 small subunit / Acetohydroxy-acid synthase I small subunit / AHAS-I / ALS-I


Mass: 11262.869 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 / Gene: b3670, ilvN, JW3645 / Production host: Escherichia coli (E. coli) / References: UniProt: P0ADF8, acetolactate synthase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1222D 1H-13C HSQC
1323D HNCA
1423D HN(CO)CA
1523D trHNCACB
1623D trCBCA(CO)NH
1723D HNCO
1823D HBHA(CO)NH
1923D (H)CCH-COSY
11023D (H)CCH-TOCSY
11122D (HB)CB(CGCD)HD
11222D (HB)CB(CGCDCE)HE
11322D tr 1H-13C HSQC (AROMATIC)
11413D 1H-15N NOESY
11523D 1H-13C NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
10.4mM [U-98% 15N] IlvN-1, 20mM potassium phosphate-2, 20mM sodium chloride-3, 1mM EDTA-4, 0.01% sodium azide-5, 5mM L-Valine-6, 90% H2O-7, 10% D2O-8, 90% H2O/10% D2O90% H2O/10% D2O
20.4mM [U-98% 13C; U-98% 15N] IlvN-9, 20mM potassium phosphate-10, 20mM sodium chloride-11, 1mM EDTA-12, 0.01% sodium azide-13, 5mM L-Valine-14, 90% H2O-15, 10% D2O-16, 90% H2O/10% D2O90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.4 mMIlvN-1[U-98% 15N]1
20 mMpotassium phosphate-21
20 mMsodium chloride-31
1 mMEDTA-41
0.01 %sodium azide-51
5 mML-Valine-61
90 %H2O-71
10 %D2O-81
0.4 mMIlvN-9[U-98% 13C; U-98% 15N]2
20 mMpotassium phosphate-102
20 mMsodium chloride-112
1 mMEDTA-122
0.01 %sodium azide-132
5 mML-Valine-142
90 %H2O-152
10 %D2O-162
Sample conditionspH: 7 / Pressure: 1 atm / Temperature: 303 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz

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Processing

NMR software
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
ANSIGKraulisdata analysis
XwinNMRBruker Biospincollection
TopSpinBruker Biospincollection
TALOSCornilescu, Delaglio and Baxdata analysis
PSVSBhattacharya and Montelionedata analysis
MOLMOLKoradi, Billeter and Wuthrichdata analysis
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR constraintsNOE constraints total: 2770 / NOE intraresidue total count: 1292 / NOE long range total count: 463 / NOE medium range total count: 312 / NOE sequential total count: 665 / Hydrogen bond constraints total count: 144 / Protein phi angle constraints total count: 180 / Protein psi angle constraints total count: 184
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1

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