1pzs
From Proteopedia
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|PDB= 1pzs |SIZE=350|CAPTION= <scene name='initialview01'>1pzs</scene>, resolution 1.63Å | |PDB= 1pzs |SIZE=350|CAPTION= <scene name='initialview01'>1pzs</scene>, resolution 1.63Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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] | + | |ACTIVITY= <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> |
|GENE= SODC OR RV0432 OR MT0447 OR MTCY22G10.29 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | |GENE= SODC OR RV0432 OR MT0447 OR MTCY22G10.29 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jcv|1JCV]], [[1bzo|1BZO]], [[1eso|1ESO]], [[1xso|1XSO]], [[1eqw|1EQW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pzs OCA], [http://www.ebi.ac.uk/pdbsum/1pzs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pzs RCSB]</span> | ||
}} | }} | ||
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[[Category: Spagnolo, L.]] | [[Category: Spagnolo, L.]] | ||
[[Category: Toro, I.]] | [[Category: Toro, I.]] | ||
| - | [[Category: CU]] | ||
[[Category: antioxidant]] | [[Category: antioxidant]] | ||
[[Category: beta core]] | [[Category: beta core]] | ||
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[[Category: metal binding]] | [[Category: metal binding]] | ||
| - | ''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 23:06:51 2008'' |
Revision as of 20:06, 30 March 2008
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| , resolution 1.63Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | SODC OR RV0432 OR MT0447 OR MTCY22G10.29 (Mycobacterium tuberculosis) | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Related: | 1JCV, 1BZO, 1ESO, 1XSO, 1EQW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of a Cu-Zn Superoxide Dismutase from Mycobacterium tuberculosis at 1.63 resolution
Overview
The sodC-encoded Mycobacterium tuberculosis superoxide dismutase (SOD) shows high sequence homology to other members of the copper/zinc-containing SOD family. Its three-dimensional structure is reported here, solved by x-ray crystallography at 1.63-A resolution. Metal analyses of the recombinant protein indicate that the native form of the enzyme lacks the zinc ion, which has a very important structural and functional role in all other known enzymes of this class. The absence of zinc within the active site is due to significant rearrangements in the zinc subloop, including deletion or mutation of the metal ligands His115 and His123. Nonetheless, the enzyme has a catalytic rate close to the diffusion limit; and unlike all other copper/zinc-containing SODs devoid of zinc, the geometry of the copper site is pH-independent. The protein shows a novel dimer interface characterized by a long and rigid loop, which confers structural stability to the enzyme. As the survival of bacterial pathogens within their host critically depends on their ability to recruit zinc in highly competitive environments, we propose that the observed structural rearrangements are required to build up a zinc-independent but fully active and stable copper-containing SOD.
About this Structure
1PZS is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site., Spagnolo L, Toro I, D'Orazio M, O'Neill P, Pedersen JZ, Carugo O, Rotilio G, Battistoni A, Djinovic-Carugo K, J Biol Chem. 2004 Aug 6;279(32):33447-55. Epub 2004 May 23. PMID:15155722
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