1q0f: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1q0f]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_seoulensis Streptomyces seoulensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0F FirstGlance]. <br>
<table><tr><td colspan='2'>[[1q0f]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_seoulensis Streptomyces seoulensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q0F FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3NI:NICKEL+(III)+ION'>3NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3NI:NICKEL+(III)+ION'>3NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q0d|1q0d]], [[1q0g|1q0g]], [[1q0k|1q0k]], [[1q0m|1q0m]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1q0d|1q0d]], [[1q0g|1q0g]], [[1q0k|1q0k]], [[1q0m|1q0m]]</td></tr>
<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q0f RCSB], [http://www.ebi.ac.uk/pdbsum/1q0f PDBsum]</span></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=1q0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q0f RCSB], [http://www.ebi.ac.uk/pdbsum/1q0f PDBsum]</span></td></tr>
<table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Streptomyces seoulensis]]
[[Category: Streptomyces seoulensis]]
[[Category: Superoxide dismutase]]
[[Category: Superoxide dismutase]]
[[Category: Carugo, K Djinovic.]]
[[Category: Carugo, K Djinovic]]
[[Category: Kang, S O.]]
[[Category: Kang, S O]]
[[Category: Lee, J W.]]
[[Category: Lee, J W]]
[[Category: Wuerges, J.]]
[[Category: Wuerges, J]]
[[Category: Yim, H S.]]
[[Category: Yim, H S]]
[[Category: Yim, Y I.]]
[[Category: Yim, Y I]]
[[Category: Homohexamer of four-helix bundle]]
[[Category: Homohexamer of four-helix bundle]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]

Revision as of 10:57, 6 January 2015

Crystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after partial x-ray-induced reductionCrystal structure of Ni-containing superoxide dismutase with Ni-ligation corresponding to the state after partial x-ray-induced reduction

Structural highlights

1q0f is a 12 chain structure with sequence from Streptomyces seoulensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Superoxide dismutase, with EC number 1.15.1.1
Resources:FirstGlance, OCA, RCSB, PDBsum

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, EC 1.15.1.1) are ubiquitous enzymes that efficiently catalyze the dismutation of superoxide radical anions to protect biological molecules from oxidative damage. The crystal structure of nickel-containing SOD (NiSOD) from Streptomyces seoulensis was determined for the resting, x-ray-reduced, and thiosulfate-reduced enzyme state. NiSOD is a homohexamer consisting of four-helix-bundle subunits. The catalytic center resides in the N-terminal active-site loop, where a Ni(III) ion is coordinated by the amino group of His-1, the amide group of Cys-2, two thiolate groups of Cys-2 and Cys-6, and the imidazolate of His-1 as axial ligand that is lost in the chemically reduced state as well as after x-ray-induced reduction. This structure represents a third class of SODs concerning the catalytic metal species, subunit structure, and oligomeric organization. It adds a member to the small number of Ni-metalloenzymes and contributes with its Ni(III) active site to the general understanding of Ni-related biochemistry. NiSOD is shown to occur also in bacteria other than Streptomyces and is predicted to be present in some cyanobacteria.

Crystal structure of nickel-containing superoxide dismutase reveals another type of active site.,Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:15173586[1]

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

See Also

References

  1. Wuerges J, Lee JW, Yim YI, Yim HS, Kang SO, Djinovic Carugo K. Crystal structure of nickel-containing superoxide dismutase reveals another type of active site. Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8569-74. Epub 2004 Jun 1. PMID:15173586 doi:http://dx.doi.org/10.1073/pnas.0308514101

1q0f, resolution 2.20Å

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