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- SASDF76: Polyphosphate-targeting protein A (PptA) -

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Basic information

Entry
Database: SASBDB / ID: SASDF76
SamplePolyphosphate-targeting protein A
  • Polyphosphate-targeting protein A (protein), PptA, Streptomyces chartreusis
Function / homologyCHAD domain superfamily / CHAD domain / CHAD / CHAD domain / CHAD domain profile. / CHAD domain protein
Function and homology information
Biological speciesStreptomyces chartreusis (bacteria)
CitationJournal: FEBS Lett / Year: 2019
Title: Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate- and metal-binding fold.
Authors: Sebastiaan Werten / Nils Hinnerk Rustmeier / Maximilian Gemmer / Marie-Joëlle Virolle / Winfried Hinrichs /
Abstract: X-ray crystallographic analysis of a phosin (PptA) from Steptomyces chartreusis reveals a metal-associated, lozenge-shaped fold featuring a 5-10 Å wide, positively charged tunnel that traverses the ...X-ray crystallographic analysis of a phosin (PptA) from Steptomyces chartreusis reveals a metal-associated, lozenge-shaped fold featuring a 5-10 Å wide, positively charged tunnel that traverses the protein core. Two distinct metal-binding sites were identified in which the predominant metal ion was Cu . In solution, PptA forms stable homodimers that bind with nanomolar affinity to polyphosphate, a stress-related biopolymer acting as a phosphate and energy reserve in conditions of nutrient depletion. A single protein dimer interacts with 14-15 consecutive phosphate moieties within the polymer. Our observations suggest that PptA plays a role in polyphosphate metabolism, mobilisation or sensing, possibly by acting in concert with polyphosphate kinase (Ppk). Like Ppk, phosins may influence antibiotic synthesis by streptomycetes.
Contact author
  • Sebastiaan Werten (Medical University of Innsbruck, Innsbruck, Austria)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #2974
Type: mix / Radius of dummy atoms: 1.90 A / Symmetry: p2 / Chi-square value: 1.06 / P-value: 0.555714
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Polyphosphate-targeting protein A / Specimen concentration: 1.31-5.48
BufferName: 20 mM Tris-HCl 400 mM NaCl / pH: 7.4
Entity #1631Name: PptA / Type: protein / Description: Polyphosphate-targeting protein A / Formula weight: 39.59 / Num. of mol.: 2 / Source: Streptomyces chartreusis / References: UniProt: A0A2N9BBV4
Sequence: GHMAQRHLDP TDPLAGPSPT GDTLAGYLRA QATEFLRALR LHRETGSGAN GAEGPVEAAR ALRRSARRIS ATLHTFQSLL DTDWCEGMRP ELAWVSGTLA MEHAYTARLE RLLNALHRLS GSTALPSQTA DSAAGGRAAG AAPVPRTAAP RDAGLRTPPT STTERGNLTV ...Sequence:
GHMAQRHLDP TDPLAGPSPT GDTLAGYLRA QATEFLRALR LHRETGSGAN GAEGPVEAAR ALRRSARRIS ATLHTFQSLL DTDWCEGMRP ELAWVSGTLA MEHAYTARLE RLLNALHRLS GSTALPSQTA DSAAGGRAAG AAPVPRTAAP RDAGLRTPPT STTERGNLTV GAAKAGALLD RQLTLARTRA HSTALQAMGS SRFHAIADKV AVLASEVPLT PAAATADLRP LATAAKDRLT DAVAALPLIT AGHPYNAAAL IHGLSPDTVP HPQDAPWHQV RLLLRLHRYA REAVSGPKGN AVVDLRLLSA GQALNRHRDA SEAAAAAAQA ARTPRIAPAT AYALGVLHAD QRHEVEAARF AFQQAWQKEA EAVSTR

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Experimental information

BeamInstrument name: PETRA III EMBL P12 / City: Hamburg / : Germany / Type of source: X-ray synchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: Polyphosphate-targeting protein A / Measurement date: Nov 24, 2016 / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.0334 3.4982
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1056 /
MinMax
Q0.0792223 2.27864
P(R) point1 1056
R0 11.84
Result
Type of curve: merged
ExperimentalStandardPorod
MW78.5 kDa58.8 kDa77.3 kDa
Volume--123.74 nm3

P(R)GuinierGuinier error
Forward scattering, I04523 4530.06 11.91
Radius of gyration, Rg3.536 nm3.51 nm0.28

MinMax
D-11.84
Guinier point23 162

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