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Yorodumi- SASDB35: Staphylococcus aureus thiaminase II (Thiaminase type II enzyme, S... -
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-Basic information
Entry | Database: SASBDB / ID: SASDB35 |
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Sample | Staphylococcus aureus thiaminase II
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Function / homology | aminopyrimidine aminohydrolase / Thiaminase II / thiaminase activity / Thiaminase-2/PQQC / TENA/THI-4/PQQC family / thiamine diphosphate biosynthetic process / Haem oxygenase-like, multi-helical / thiamine biosynthetic process / Aminopyrimidine aminohydrolase Function and homology information |
Biological species | Staphylococcus aureus (bacteria) |
Citation | Journal: 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 |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-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
Sample | Name: Staphylococcus aureus thiaminase II / Specimen concentration: 1.20-7.20 |
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Buffer | Name: 100 mM Tris-HCl / pH: 7.5 |
Entity #353 | Name: 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 |
-Experimental information
Beam | Instrument name: DORIS III EMBL X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm | |||||||||||||||||||||||||||||||||||||||
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Detector | Name: 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 /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 809 /
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Result | Type of curve: extrapolated
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