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- SASDBZ5: Enzyme I-Ntr (residues 170-424) in complex with NPr (residues 1-85) -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDBZ5
SampleEnzyme I-Ntr (residues 170-424) in complex with NPr (residues 1-85)
  • Phosphocarrier protein NPr (protein), NPr, Escherichia coli
  • Phosphoenolpyruvate-protein phosphotransferase PtsP (protein), Enzyme I-Ntr, Escherichia coli
Function / homology
Function and homology information


transferase activity, transferring phosphorus-containing groups / phosphoenolpyruvate-protein phosphotransferase / phosphoenolpyruvate-protein phosphotransferase activity / N-acetylglucosamine transport / phosphoenolpyruvate-dependent sugar phosphotransferase system / kinase activity / metal ion binding / cytoplasm
Similarity search - Function
Phosphotransferase system, enzyme I-like / Phosphotransferase system, enzyme I N-terminal / PtsI, HPr-binding domain superfamily / : / PEP-utilising enzyme, N-terminal / PEP-utilising enzyme, active site / PEP-utilizing enzymes phosphorylation site signature. / PEP-utilising enzyme, conserved site / PEP-utilizing enzymes signature 2. / PEP-utilising enzyme, C-terminal ...Phosphotransferase system, enzyme I-like / Phosphotransferase system, enzyme I N-terminal / PtsI, HPr-binding domain superfamily / : / PEP-utilising enzyme, N-terminal / PEP-utilising enzyme, active site / PEP-utilizing enzymes phosphorylation site signature. / PEP-utilising enzyme, conserved site / PEP-utilizing enzymes signature 2. / PEP-utilising enzyme, C-terminal / PEP-utilising enzyme, PEP-binding domain / Phosphotransferase system, HPr histidine phosphorylation site / PTS HPR domain histidine phosphorylation site signature. / Phosphotransferase system, HPr serine phosphorylation site / PEP-utilising enzyme, mobile domain / Phosphohistidine domain superfamily / PEP-utilising enzyme, mobile domain / Phosphocarrier protein HPr-like / HPr-like superfamily / : / PTS HPr component phosphorylation site / PTS HPR domain profile. / PTS HPR domain serine phosphorylation site signature. / Pyruvate kinase-like domain superfamily / Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily / GAF domain / Domain present in phytochromes and cGMP-specific phosphodiesterases. / GAF domain / GAF-like domain superfamily
Similarity search - Domain/homology
Phosphocarrier protein NPr / Phosphoenolpyruvate-dependent phosphotransferase system
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
CitationDate: 2016 Nov 8
Title: Structure of the NPr:EIN-Ntr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.
Authors: Strickland M / Stanley AM / Wang G / Botos I / Schwieters CD / Buchanan SK / Peterkofsky A
Contact author
  • Madeleine Strickland (NIH, National Institutes of Health, Bethesda, MD, Bethesda, Maryland, USA)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #893
Type: atomic / Software: CRYSOL (2.8.3) / Comment: Fig. 5J / Chi-square value: 1.248
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Enzyme I-Ntr (residues 170-424) in complex with NPr (residues 1-85)
Specimen concentration: 3.76 mg/ml / Entity id: 390 / 391
BufferName: 10 mM Tris 150 mM NaCl 0.5 mM EDTA / pH: 7.5
Entity #390Name: NPr / Type: protein / Description: Phosphocarrier protein NPr / Formula weight: 9.25 / Num. of mol.: 1 / Source: Escherichia coli / References: UniProt: P0A9N0
Sequence:
MTVKQTVEIT NKLGMHARPA MKLFELMQGF DAEVLLRNDE GTEAEANSVI ALLMLDSAKG RQIEVEATGP QEEEALAAVI ALFNS
Entity #391Name: Enzyme I-Ntr / Type: protein
Description: Phosphoenolpyruvate-protein phosphotransferase PtsP
Formula weight: 28.35 / Num. of mol.: 1 / Source: Escherichia coli / References: UniProt: P37177
Sequence: RIRALPAAPG VAIAEGWQDA TLPLMEQVYQ ASTLDPALER ERLTGALEEA ANEFRRYSKR FAAGAQKETA AIFDLYSHLL SDTRLRRELF AEVDKGSVAE WAVKTVIEKF AEQFAALSDN YLKERAGDLR ALGQRLLFHL DDANQGPNAW PERFILVADE LSATTLAELP ...Sequence:
RIRALPAAPG VAIAEGWQDA TLPLMEQVYQ ASTLDPALER ERLTGALEEA ANEFRRYSKR FAAGAQKETA AIFDLYSHLL SDTRLRRELF AEVDKGSVAE WAVKTVIEKF AEQFAALSDN YLKERAGDLR ALGQRLLFHL DDANQGPNAW PERFILVADE LSATTLAELP QDRLVGVVVR DGAANSHAAI MVRALGIPTV MGADIQPSVL HRRTLIVDGY RGELLVDPEP VLLQEYQRLI SEEIELSRLA EDDVN

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Experimental information

BeamInstrument name: NIDDK, NIH / City: Bethesda, MD / 国: USA / Type of source: X-ray in house / Wavelength: 0.154 Å
Scan
Title: Enzyme I-Ntr (residues 170-424) in complex with NP / Measurement date: Jan 30, 2015 / Storage temperature: 4 °C / Cell temperature: 27 °C / Exposure time: 1800 sec. / Number of frames: 8 / Unit: 1/A /
MinMax
Q0.0181 0.6797
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 214 /
MinMax
Q0.032546 0.339536
P(R) point1 214
R0 81.56
Result
Type of curve: single_conc
ExperimentalStandardPorod
MW37.6 kDa22 kDa30.6 kDa
Volume--52 nm3

P(R)Guinier
Forward scattering, I02.87 2.83
Radius of gyration, Rg2.373 nm2.319 nm

MinMax
D-8.16
Guinier point7 25

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