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- SASDB35: Staphylococcus aureus thiaminase II (Thiaminase type II enzyme, S... -

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Basic information

Entry
Database: SASBDB / ID: SASDB35
SampleStaphylococcus aureus thiaminase II
  • Thiaminase type II enzyme (protein), SaTenA, Staphylococcus aureus
Function / homology
Function and homology information


aminopyrimidine aminohydrolase / thiaminase activity / thiamine biosynthetic process / thiamine diphosphate biosynthetic process / cytosol
Similarity search - Function
Thiaminase II / : / Thiaminase-2/PQQC / TENA/THI-4/PQQC family / Haem oxygenase-like, multi-helical
Similarity search - Domain/homology
Aminopyrimidine aminohydrolase
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
CitationJournal: Acta Crystallogr D Biol Crystallogr / Year: 2013
Title: Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic protection against serine proteases.
Authors: Afshan Begum / Julia Drebes / Alexey Kikhney / Ingrid B Müller / Markus Perbandt / Dmitri Svergun / Carsten Wrenger / Christian Betzel /
Abstract: Staphylococcus aureus TenA (SaTenA) is a thiaminase type II enzyme that catalyzes the deamination of aminopyrimidine, as well as the cleavage of thiamine into 4-amino-5-hydroxymethyl-2- ...Staphylococcus aureus TenA (SaTenA) is a thiaminase type II enzyme that catalyzes the deamination of aminopyrimidine, as well as the cleavage of thiamine into 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) and 5-(2-hydroxyethyl)-4-methylthiazole (THZ), within thiamine (vitamin B1) metabolism. Further, by analogy with studies of Bacillus subtilis TenA, SaTenA may act as a regulator controlling the secretion of extracellular proteases such as the subtilisin type of enzymes in bacteria. Thiamine biosynthesis has been identified as a potential drug target of the multi-resistant pathogen S. aureus and therefore all enzymes involved in the S. aureus thiamine pathway are presently being investigated in detail. Here, the structure of SaTenA, determined by molecular replacement and refined at 2.7 Å resolution to an R factor of 21.6% with one homotetramer in the asymmetric unit in the orthorhombic space group P212121, is presented. The tetrameric state of wild-type (WT) SaTenA was postulated to be the functional biological unit and was confirmed by small-angle X-ray scattering (SAXS) experiments in solution. To obtain insights into structural and functional features of the oligomeric SaTenA, comparative kinetic investigations as well as experiments analyzing the structural stability of the WT SaTenA tetramer versus a monomeric SaTenA mutant were performed.
Contact author
  • Al Kikhney (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #549
Type: atomic / Software: (2.8.2) / Symmetry: P222 / Chi-square value: 1.218816
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Staphylococcus aureus thiaminase II / Specimen concentration: 1.20-7.20
BufferName: 100 mM Tris-HCl / pH: 7.5
Entity #353Name: SaTenA / Type: protein / Description: Thiaminase type II enzyme / Formula weight: 26.84 / Num. of mol.: 4 / Source: Staphylococcus aureus / References: UniProt: Q6GEY1
Sequence: MEFSQKLYQA AKPIINDIYE DDFIQKMLLG NIQADALRHY LQADAAYLKE FTNLYALLIP KMNSMNDVKF LVEQIEFMVE GEVLAHDILA QIVGESYEEI IKTKVWPPSG DHYIKHMYFQ AHSRENAIYT IAAMAPCPYI YAELAKRSQS DHKLNREKDT AKWFDFYSTE ...Sequence:
MEFSQKLYQA AKPIINDIYE DDFIQKMLLG NIQADALRHY LQADAAYLKE FTNLYALLIP KMNSMNDVKF LVEQIEFMVE GEVLAHDILA QIVGESYEEI IKTKVWPPSG DHYIKHMYFQ AHSRENAIYT IAAMAPCPYI YAELAKRSQS DHKLNREKDT AKWFDFYSTE MDDIINVFES LMNKLAESMS DKELEQVKQV FLESCIHERR FFNMAMTLEQ WEFGGKVND

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Experimental information

BeamInstrument name: DORIS III EMBL X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm
DetectorName: Pilatus 1M-W / Pixsize x: 0.172 mm
Scan
Title: SaTenA / Measurement date: May 11, 2011 / Cell temperature: 5 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /
MinMax
Q0.171 6.0241
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 809 /
MinMax
Q0.171034 2.38372
P(R) point1 809
R0 11
Result
Type of curve: extrapolated
ExperimentalExperimental errorPorodPorod error
MW105 kDa20 105 kDa20
Volume--168 nm3-

P(R)GuinierGuinier error
Forward scattering, I083.43 84.12 -
Radius of gyration, Rg3.33 nm3.35 nm0.2

MinMaxError
D-11 1
Guinier point1 80 -

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