000			01989 a2200493 4500
005			20250515161306.0
264		0	_c20090717
008			200907s 0 0 eng d
022			_a1399-0047
024	7		_a10.1107/S0907444908043023 _2doi
040			_aNLM _beng _cNLM
100	1		_aCarius, Yvonne
245	0	0	_aThe structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation. _h[electronic resource]
260			_bActa crystallographica. Section D, Biological crystallography _cMar 2009
300			_a229-40 p. _bdigital
500			_aPublication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
650	0	4	_aAmino Acid Motifs
650	0	4	_aAmino Acid Sequence
650	0	4	_aBacterial Proteins _xchemistry
650	0	4	_aBinding Sites
650	0	4	_aCrystallography, X-Ray
650	0	4	_aDimerization
650	0	4	_aDisulfides _xmetabolism
650	0	4	_aGlutaredoxins _xchemistry
650	0	4	_aModels, Molecular
650	0	4	_aMolecular Sequence Data
650	0	4	_aOxidation-Reduction
650	0	4	_aOxidoreductases Acting on Sulfur Group Donors _xmetabolism
650	0	4	_aParacoccus pantotrophus _xenzymology
650	0	4	_aProtein Conformation
650	0	4	_aProtein Disulfide Reductase (Glutathione) _xchemistry
650	0	4	_aRecombinant Fusion Proteins _xchemistry
650	0	4	_aSelenomethionine _xchemistry
650	0	4	_aSequence Alignment
650	0	4	_aSequence Homology, Amino Acid
650	0	4	_aStructure-Activity Relationship
650	0	4	_aSulfur _xmetabolism
650	0	4	_aThioredoxins _xchemistry
700	1		_aRother, Dagmar
700	1		_aFriedrich, Cornelius G
700	1		_aScheidig, Axel J
773	0		_tActa crystallographica. Section D, Biological crystallography _gvol. 65 _gno. Pt 3 _gp. 229-40
856	4	0	_uhttps://doi.org/10.1107/S0907444908043023 _zAvailable from publisher's website
999			_c18679922 _d18679922