This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3ce1

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal Structure of the Cu/Zn Superoxide Dismutase from Cryptococcus liquefaciens Strain N6

Structural highlights

3ce1 is a 1 chain structure with sequence from Naganishia liquefaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0ZPR9_9TREE Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).[RuleBase:RU000393]

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

The deep-sea yeast Cryptococcus liquefaciens strain N6 shows high tolerance towards heavy metals, and can grow in the presence of high concentrations of copper ions. Enzymatic analysis indicated that copper ions induced the Cu/Zn superoxide dismutase activity of strain N6 (Cl-SOD1). In this study, the 1.2A resolution crystal structure of Cl-SOD1 has revealed several significant residue substitutions compared to the other Cu/Zn SODs. In the electrostatic loop, notably, His135 and Pro136 replace the well-conserved linear residues, while Thr133 substitutes a highly conserved glycine. The electrostatic loop has been shown to be involved in the copper uptake process, and these substitutions have caused an inward dragging of the turn region of the loop. As the introduction of proline and abolishment of glycine decrease loop flexibility, this structural reorganization may have helped stabilize the loop conformation, possibly resulting in more efficient copper uptake and a more stabilized copper-bound form.

Structure of Cu/Zn superoxide dismutase from the heavy-metal-tolerant yeast Cryptococcus liquefaciens strain N6.,Teh AH, Kanamasa S, Kajiwara S, Kumasaka T Biochem Biophys Res Commun. 2008 Sep 26;374(3):475-8. Epub 2008 Jul 18. PMID:18640099^[1]

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

References

↑ Teh AH, Kanamasa S, Kajiwara S, Kumasaka T. Structure of Cu/Zn superoxide dismutase from the heavy-metal-tolerant yeast Cryptococcus liquefaciens strain N6. Biochem Biophys Res Commun. 2008 Sep 26;374(3):475-8. Epub 2008 Jul 18. PMID:18640099 doi:10.1016/j.bbrc.2008.07.046

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/3ce1"

@@ Line 3: / Line 3: @@
 <StructureSection load='3ce1' size='340' side='right'caption='[[3ce1]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ce1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_32060 Atcc 32060]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CE1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ce1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naganishia_liquefaciens Naganishia liquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CE1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C-SOD1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=104408 ATCC 32060])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </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=3ce1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ce1 OCA], [https://pdbe.org/3ce1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ce1 RCSB], [https://www.ebi.ac.uk/pdbsum/3ce1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ce1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/A0ZPR9_9TREE A0ZPR9_9TREE]] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).[RuleBase:RU000393]
+[https://www.uniprot.org/uniprot/A0ZPR9_9TREE A0ZPR9_9TREE] Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity).[RuleBase:RU000393]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 32060]]
 [[Category: Large Structures]]
-[[Category: Superoxide dismutase]]
+[[Category: Naganishia liquefaciens]]
-[[Category: Kajiwara, S]]
+[[Category: Kajiwara S]]
-[[Category: Kanamasa, S]]
+[[Category: Kanamasa S]]
-[[Category: Kumasaka, T]]
+[[Category: Kumasaka T]]
-[[Category: Teh, A H]]
+[[Category: Teh AH]]
-[[Category: Antioxidant]]
-[[Category: Copper]]
-[[Category: Greek-key beta barrel]]
-[[Category: Metal-binding]]
-[[Category: Oxidoreductase]]
-[[Category: Zinc]]

3ce1

From Proteopedia

Current revision

Crystal Structure of the Cu/Zn Superoxide Dismutase from Cryptococcus liquefaciens Strain N6

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox