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- SASDGX6: Cysteine synthase/Serine acetyltransferase complex -

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ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDGX6
SampleCysteine synthase/Serine acetyltransferase complex
  • Cysteine synthase A (4-mer) (protein), CysK, Escherichia coli
  • Serine acetyltransferase (6-mer) (protein), CysE, Escherichia coli
Function / homology
Function and homology information


S-carboxymethylcysteine synthase / S-carboxymethylcysteine synthase activity / cysteine synthase complex / serine O-acetyltransferase / serine O-acetyltransferase activity / cystathionine beta-synthase activity / cysteine synthase / L-cysteine desulfhydrase activity / cysteine synthase activity / cysteine biosynthetic process from serine ...S-carboxymethylcysteine synthase / S-carboxymethylcysteine synthase activity / cysteine synthase complex / serine O-acetyltransferase / serine O-acetyltransferase activity / cystathionine beta-synthase activity / cysteine synthase / L-cysteine desulfhydrase activity / cysteine synthase activity / cysteine biosynthetic process from serine / amino acid biosynthetic process / response to X-ray / pyridoxal phosphate binding / transferase activity / protein homodimerization activity / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Serine acetyltransferase, LbH domain / Serine O-acetyltransferase / Serine acetyltransferase, N-terminal / Serine acetyltransferase, N-terminal / Serine acetyltransferase, N-terminal / Serine acetyltransferase, N-terminal domain superfamily / Cysteine synthase CysK / Cysteine synthase / Cysteine synthase/cystathionine beta-synthase, pyridoxal-phosphate attachment site / Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. ...Serine acetyltransferase, LbH domain / Serine O-acetyltransferase / Serine acetyltransferase, N-terminal / Serine acetyltransferase, N-terminal / Serine acetyltransferase, N-terminal / Serine acetyltransferase, N-terminal domain superfamily / Cysteine synthase CysK / Cysteine synthase / Cysteine synthase/cystathionine beta-synthase, pyridoxal-phosphate attachment site / Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. / Hexapeptide transferase, conserved site / Hexapeptide-repeat containing-transferases signature. / Hexapeptide repeat / Bacterial transferase hexapeptide (six repeats) / Pyridoxal-phosphate dependent enzyme / Tryptophan synthase beta subunit-like PLP-dependent enzyme / Pyridoxal-phosphate dependent enzyme / Trimeric LpxA-like superfamily
Similarity search - Domain/homology
Serine acetyltransferase / Cysteine synthase A
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
CitationDate: 2019 Oct 21
Title: Combination of SAXS and Protein Painting Discloses the Three-Dimensional Organization of the Bacterial Cysteine Synthase Complex, a Potential Target for Enhancers of Antibiotic Action
Authors: Rosa B / Marchetti M / Paredi G / Amenitsch H / Franko N / Benoni R / Giabbai B / De Marino M / Mozzarelli A / Ronda L / Storici P / Campanini B
Contact author
  • Heinz Amenitsch (Graz University of Technology)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #3854
Type: dummy / Radius of dummy atoms: 3.75 A / Chi-square value: 1.885 / P-value: 0.423693
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Cysteine synthase/Serine acetyltransferase complex / Specimen concentration: 0.50-1.50 / Entity id: 1933 / 1934
BufferName: 20 mM sodium phosphate, 85 mM NaCl, 2 mM EDTA, 10 mM 2-MCE
pH: 7.5
Entity #1933Name: CysK / Type: protein / Description: Cysteine synthase A (4-mer) / Formula weight: 35.712 / Num. of mol.: 4 / Source: Escherichia coli / References: UniProt: P0ABK5
Sequence: MGKIFEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI WDAEKRGVLK PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER RKLLKALGAN LVLTEGAKGM KGAIQKAEEI VASNPEKYLL LQQFSNPANP EIHEKTTGPE IWEDTDGQVD ...Sequence:
MGKIFEDNSL TIGHTPLVRL NRIGNGRILA KVESRNPSFS VKCRIGANMI WDAEKRGVLK PGVELVEPTS GNTGIALAYV AAARGYKLTL TMPETMSIER RKLLKALGAN LVLTEGAKGM KGAIQKAEEI VASNPEKYLL LQQFSNPANP EIHEKTTGPE IWEDTDGQVD VFIAGVGTGG TLTGVSRYIK GTKGKTDLIS VAVEPTDSPV IAQALAGEEI KPGPHKIQGI GAGFIPANLD LKLVDKVIGI TNEEAISTAR RLMEEEGILA GISSGAAVAA ALKLQEDESF TNKNIVVILP SSGERYLSTA LFADLFTEKE LQQTSLEHHH HHH
Entity #1934Name: CysE / Type: protein / Description: Serine acetyltransferase (6-mer) / Formula weight: 29.43 / Num. of mol.: 6 / Source: Escherichia coli / References: UniProt: P0A9D4
Sequence: SGTSCEELEI VWNNIKAEAR TLADCEPMLA SFYHATLLKH ENLGSALSYM LANKLSSPIM PAIAIREVVE EAYAADPEMI ASAACDIQAV RTRDPAVDKY STPLLYLKGF HALQAYRIGH WLWNQGRRAL AIFLQNQVSV TFQVDIHPAA KIGRGIMLDH ATGIVVGETA ...Sequence:
SGTSCEELEI VWNNIKAEAR TLADCEPMLA SFYHATLLKH ENLGSALSYM LANKLSSPIM PAIAIREVVE EAYAADPEMI ASAACDIQAV RTRDPAVDKY STPLLYLKGF HALQAYRIGH WLWNQGRRAL AIFLQNQVSV TFQVDIHPAA KIGRGIMLDH ATGIVVGETA VIENDVSILQ SVTLGGTGKS GGDRHPKIRE GVMIGAGAKI LGNIEVGRGA KIGAGSVVLQ PVPPHTTAAG VPARIVGKPD SDKPSMDMDQ HFNGINHTFE YGDGI

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Experimental information

BeamInstrument name: ELETTRA - Sincrotrone Trieste Austrian SAXS beamline 5.2L
City: Trieste / 国: Italy / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.154 Å / Dist. spec. to detc.: 1.2324 mm
DetectorName: Dectris / Pilatus3 1M / Pixsize x: 0.172 mm
Scan
Title: Cysteine synthase/Serine acetyltransferase complex / Measurement date: Jun 1, 2016 / Storage temperature: 4 °C / Cell temperature: 20 °C / Exposure time: 10 sec. / Number of frames: 12 / Unit: 1/nm /
MinMax
Q0.1384 3.4999
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 298 /
MinMax
Q0.1412 3.497
P(R) point1 298
R0 22
Result
Type of curve: merged /
ExperimentalPorod
MW303 kDa290 kDa
Volume-457 nm3

P(R)GuinierGuinier error
Forward scattering, I027.99 26.97 0.24
Radius of gyration, Rg6.6 nm6.1 nm0.11

MinMax
D-22
Guinier point1 14

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