2w7w

From Proteopedia

(Difference between revisions)

Current revision

The crystal structure of iron superoxide dismutase from Aliivibrio salmonicida.

Structural highlights

2w7w is a 2 chain structure with sequence from Aliivibrio salmonicida LFI1238. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B6ENP9_ALISL Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Superoxide dismutases (SODs) are metalloenzymes that catalyse the dismutation of the superoxide radical anion into O(2) and H(2)O(2) in a two-step reaction. The crystal structure of the iron superoxide dismutase from the cold-adapted and fish-pathogenic bacterium Aliivibrio salmonicida (asFeSOD) has been determined and refined to 1.7 A resolution. The protein has been characterized and compared with the closely related homologous iron superoxide dismutase from the mesophilic Escherichia coli (ecFeSOD) in an attempt to rationalize its environmental adaptation. ecFeSOD shares 75% identity with asFeSOD. Compared with the mesophilic FeSOD, the psychrophilic FeSOD has distinct temperature differences in residual activity and thermostability that do not seem to be related to structural differences such as intramolecular or intermolecular ion bonds, hydrogen bonds or cavity sizes. However, an increased net negative charge on the surface of asFeSOD may explain its lower thermostability compared with ecFeSOD. Activity measurements and differential scanning calorimetry measurements revealed that the psychrophilic asFeSOD had a thermostability that was significantly higher than the optimal growth temperature of the host organism.

The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD from Aliivibrio salmonicida.,Pedersen HL, Willassen NP, Leiros I Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt, 2):84-92. Epub 2009 Jan 31. PMID:19193992^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pedersen HL, Willassen NP, Leiros I. The first structure of a cold-adapted superoxide dismutase (SOD): biochemical and structural characterization of iron SOD from Aliivibrio salmonicida. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt, 2):84-92. Epub 2009 Jan 31. PMID:19193992 doi:http://dx.doi.org/10.1107/S1744309109001110

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2w7w"

Categories: Aliivibrio salmonicida LFI1238 | Large Structures | Leiros I | Pedersen HL | Willassen NP

@@ Line 1: / Line 1: @@
 ==The crystal structure of iron superoxide dismutase from Aliivibrio salmonicida.==
-<StructureSection load='2w7w' size='340' side='right' caption='[[2w7w]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+<StructureSection load='2w7w' size='340' side='right'caption='[[2w7w]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2w7w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Alisl Alisl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2W7W FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2w7w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliivibrio_salmonicida_LFI1238 Aliivibrio salmonicida LFI1238]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W7W FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.7&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span></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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2w7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w7w OCA], [http://pdbe.org/2w7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2w7w RCSB], [http://www.ebi.ac.uk/pdbsum/2w7w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2w7w 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=2w7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w7w OCA], [https://pdbe.org/2w7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w7w RCSB], [https://www.ebi.ac.uk/pdbsum/2w7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w7w ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/B6ENP9_ALISL B6ENP9_ALISL]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).
+[https://www.uniprot.org/uniprot/B6ENP9_ALISL B6ENP9_ALISL] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Superoxide Dismutase|Superoxide Dismutase]]
+*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Alisl]]
+[[Category: Aliivibrio salmonicida LFI1238]]
-[[Category: Superoxide dismutase]]
+[[Category: Large Structures]]
-[[Category: Leiros, I]]
+[[Category: Leiros I]]
-[[Category: Pedersen, H L]]
+[[Category: Pedersen HL]]
-[[Category: Willassen, N P]]
+[[Category: Willassen NP]]
-[[Category: Aliivibrio salmonicida]]
-[[Category: Cold adaptation]]
-[[Category: Differential scanning calorimetry]]
-[[Category: Dsc]]
-[[Category: Fesod]]
-[[Category: Oxidoreductase]]
-[[Category: Sodb]]
-[[Category: Structural analysis]]

2w7w

From Proteopedia

Current revision

The crystal structure of iron superoxide dismutase from Aliivibrio salmonicida.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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