1e9p
From Proteopedia
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|PDB= 1e9p |SIZE=350|CAPTION= <scene name='initialview01'>1e9p</scene>, resolution 1.70Å | |PDB= 1e9p |SIZE=350|CAPTION= <scene name='initialview01'>1e9p</scene>, resolution 1.70Å | ||
|SITE= <scene name='pdbsite=CU1:Cu+Binding+Site+For+Residue+A152'>CU1</scene>, <scene name='pdbsite=CU2:Cu+Binding+Site+For+Residue+A153'>CU2</scene>, <scene name='pdbsite=CU3:Cu+Binding+Site+For+Residue+B152'>CU3</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site+For+Residueb153'>ZNB</scene> | |SITE= <scene name='pdbsite=CU1:Cu+Binding+Site+For+Residue+A152'>CU1</scene>, <scene name='pdbsite=CU2:Cu+Binding+Site+For+Residue+A153'>CU2</scene>, <scene name='pdbsite=CU3:Cu+Binding+Site+For+Residue+B152'>CU3</scene> and <scene name='pdbsite=ZNB:Zn+Binding+Site+For+Residueb153'>ZNB</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Catechol_1,2-dioxygenase Catechol 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.1 1.13.11.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e9p OCA], [http://www.ebi.ac.uk/pdbsum/1e9p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e9p RCSB]</span> | ||
}} | }} | ||
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Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080458 11080458] | Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080458 11080458] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| + | [[Category: Catechol 1,2-dioxygenase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Transferred entry: 1 13 11 1]] | ||
[[Category: Hasnain, S S.]] | [[Category: Hasnain, S S.]] | ||
[[Category: Hough, M A.]] | [[Category: Hough, M A.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: ZN]] | ||
[[Category: asymmetry]] | [[Category: asymmetry]] | ||
[[Category: enzyme]] | [[Category: enzyme]] | ||
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[[Category: superoxide]] | [[Category: superoxide]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:58:18 2008'' |
Revision as of 16:58, 30 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , | ||||||
| Activity: | Catechol 1,2-dioxygenase, with EC number 1.13.11.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF BOVINE CU, ZN SOD TO 1.7 ANGSTROM (3 OF 3)
Overview
The structure of the catalytic site in one subunit of bovine CuZn superoxide dismutase is shown to be highly variable. A series of crystal structures at approximately 1.7 A have been determined using data collected from different crystals. Several conformations are observed for the copper site from one of the subunits. These conformations lie between those expected for the Cu(II) and Cu(I) forms of the enzyme and may represent a slow positional rearrangement of the Cu site during the crystallisation process due to the presence of a trace reductant in the mother liquor. These states perhaps indicate some functionally relevant structural steps that ultimately result in the breakage of the imidazolate bridge between the two metal sites.This behaviour is not observed for the second subunit of the dimeric enzyme, which remains in the five-coordinate, distorted square planar geometry in all cases. We suggest that this asymmetric behaviour may be caused by the lack of mobility for the Glu119-Leu142 loop region in the second subunit caused by crystal contacts. This region forms one wall of the active-site cavity, and its mobility has been suggested, via molecular dynamics studies, to be important for the catalytic mechanism.
About this Structure
1E9P is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
Conformational variability of the Cu site in one subunit of bovine CuZn superoxide dismutase: the importance of mobility in the Glu119-Leu142 loop region for catalytic function., Hough MA, Strange RW, Hasnain SS, J Mol Biol. 2000 Nov 24;304(2):231-41. PMID:11080458
Page seeded by OCA on Sun Mar 30 19:58:18 2008
