3sdp: Difference between revisions
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[[Image:3sdp.jpg|left|200px]] | [[Image:3sdp.jpg|left|200px]] | ||
'''THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS''' | {{Structure | ||
|PDB= 3sdp |SIZE=350|CAPTION= <scene name='initialview01'>3sdp</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3SDP is a [ | 3SDP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. The following page contains interesting information on the relation of 3SDP with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb94_1.html Superoxide Dismutase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SDP OCA]. | ||
==Reference== | ==Reference== | ||
The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis., Stoddard BL, Howell PL, Ringe D, Petsko GA, Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:[http:// | The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis., Stoddard BL, Howell PL, Ringe D, Petsko GA, Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2271564 2271564] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase (superoxide acceptor)]] | [[Category: oxidoreductase (superoxide acceptor)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:07:12 2008'' | ||
Revision as of 17:07, 20 March 2008
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| 3sdp, resolution 2.1Å | |||||||||||||
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| Ligands: | FE | ||||||||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
THE 2.1 ANGSTROMS RESOLUTION STRUCTURE OF IRON SUPEROXIDE DISMUTASE FROM PSEUDOMONAS OVALIS
Overview
The 2.1-A resolution crystal structure of native uncomplexed iron superoxide dismutase (EC 1.15.1.1) from Pseudomonas ovalis was solved and refined to a final R factor of 24%. The dimeric structure contains one catalytic iron center per monomer with an asymmetric trigonal-bipyramidal coordination of protein ligands to the metal. Each monomer contains two domains, with the trigonal ligands (histidines 74 and 160; aspartate 156) contributed by the large domain and stabilized by an extended hydrogen-bonded network, including residues from opposing monomers. The axial ligand (histidine 26) is found on the small domain and does not participate extensively in the stabilizing H-bond network. The open axial coordination position of the iron is devoid of bound water molecules or anions. The metal is located 0.5 A out of the plane of the trigonal ligands toward histidine 26, providing a slightly skewed coordination away from the iron binding site. The molecule contains a glutamine residue in the active site which is conserved between all iron enzymes sequenced to data but which is conserved among all manganese SODs at a separate position in the sequence. This residue shows the same structural interactions in both cases, implying that iron and manganese SODs are second-site revertants of one another.
About this Structure
3SDP is a Single protein structure of sequence from Pseudomonas putida. The following page contains interesting information on the relation of 3SDP with [Superoxide Dismutase]. Full crystallographic information is available from OCA.
Reference
The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis., Stoddard BL, Howell PL, Ringe D, Petsko GA, Biochemistry. 1990 Sep 25;29(38):8885-93. PMID:2271564
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