4l2b | pdb_00004l2b

X-ray structure of the C57S mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis

spinqualitylabelsall models 4l2b, resolution 1.97Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4l2b is a 2 chain structure with sequence from "alteromonas_marinopraesens"_(zobell_and_upham_1944)_baumann_et_al._1972 "alteromonas marinopraesens" (zobell and upham 1944) baumann et al. 1972. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE, TRE Related: 4l2a, 4l2c, 4l2d, 3lio, 3ljf, 3lj9 Gene: sodB, PSHAa1215 ("Alteromonas marinopraesens" (ZoBell and Upham 1944) Baumann et al. 1972) Activity: Superoxide dismutase, with EC number 1.15.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SODF_PSEHT] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Publication Abstract from PubMed A peculiar feature of the psychrophilic iron superoxide dismutase from Pseudoalteromonas haloplanktis (PhSOD) is the presence in its amino acid sequence of a reactive cysteine (Cys57). To define the role of this residue, a structural characterization of the effect of two PhSOD mutations, C57S and C57R, was performed. Thermal and denaturant-induced unfolding of wild type and mutant PhSOD followed by circular dichroism and fluorescence studies revealed that C-->R substitution alters the thermal stability and the resistance against denaturants of the enzyme, whereas C57S only alters the stability of the protein against urea. The crystallographic data on the C57R mutation suggest an involvement of the Arg side chain in the formation of salt bridges on protein surface. These findings support the hypothesis that the thermal resistance of PhSOD relies on optimization of charge-charge interactions on its surface. Our study contributes to a deeper understanding of the denaturation mechanism of superoxide dismutases, suggesting the presence of a structural dimeric intermediate between the native state and the unfolded state. This hypothesis is supported by the crystalline and solution data on the reduced form of the enzyme. Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.,Merlino A, Russo Krauss I, Castellano I, Ruocco MR, Capasso A, De Vendittis E, Rossi B, Sica F Biochim Biophys Acta. 2014 Mar;1844(3):632-40. doi: 10.1016/j.bbapap.2014.01.007., Epub 2014 Jan 17. PMID:24440460 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Superoxide Dismutase

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