4l2c: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L2C FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_haloplanktis Pseudoalteromonas haloplanktis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L2C FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.66&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4l2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2c OCA], [https://pdbe.org/4l2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l2c RCSB], [https://www.ebi.ac.uk/pdbsum/4l2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l2c ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4l2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2c OCA], [https://pdbe.org/4l2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l2c RCSB], [https://www.ebi.ac.uk/pdbsum/4l2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l2c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SODF_PSET1 SODF_PSET1] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.<ref>PMID:16713057</ref>  
[https://www.uniprot.org/uniprot/SODF_PSET1 SODF_PSET1] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.<ref>PMID:16713057</ref>  
<div style="background-color:#fffaf0;">
== 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--&gt;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<ref>PMID:24440460</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4l2c" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 15:16, 1 March 2024

X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)

Structural highlights

4l2c is a 4 chain structure with sequence from Pseudoalteromonas haloplanktis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.66Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SODF_PSET1 Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.[1]

See Also

References

  1. ↑ Castellano I, Di Maro A, Ruocco MR, Chambery A, Parente A, Di Martino MT, Parlato G, Masullo M, De Vendittis E. Psychrophilic superoxide dismutase from Pseudoalteromonas haloplanktis: biochemical characterization and identification of a highly reactive cysteine residue. Biochimie. 2006 Oct;88(10):1377-89. Epub 2006 Apr 27. PMID:16713057 doi:http://dx.doi.org/S0300-9084(06)00055-1

4l2c, resolution 1.66Å

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