2gbt
From Proteopedia
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|PDB= 2gbt |SIZE=350|CAPTION= <scene name='initialview01'>2gbt</scene>, resolution 1.700Å | |PDB= 2gbt |SIZE=350|CAPTION= <scene name='initialview01'>2gbt</scene>, resolution 1.700Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene> | + | |LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hl4|1HL4]], [[2gbu|2GBU]], [[2gbv|2GBV]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gbt OCA], [http://www.ebi.ac.uk/pdbsum/2gbt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gbt RCSB]</span> | ||
}} | }} | ||
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[[Category: Marklund, S L.]] | [[Category: Marklund, S L.]] | ||
[[Category: Oliveberg, M.]] | [[Category: Oliveberg, M.]] | ||
| - | [[Category: CU1]] | ||
| - | [[Category: ZN]] | ||
[[Category: human cu/zn superoxide dismutase]] | [[Category: human cu/zn superoxide dismutase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:14:33 2008'' |
Revision as of 00:14, 31 March 2008
| |||||||
| , resolution 1.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | SOD1 (Homo sapiens) | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Related: | 1HL4, 2GBU, 2GBV
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
C6A/C111A CuZn Superoxide dismutase
Contents |
Overview
The gain of neurotoxic function in amyotrophic lateral sclerosis (ALS) has been linked to misfolding of the homodimeric enzyme Cu/Zn superoxide dismutase (SOD). Here, we present the crystal structure of fully cysteine-depleted human SOD (SOD(CallA)), representing a reduced, marginally stable intermediate on the folding pathway in vivo that has also been implicated as neurotoxic precursor state. A hallmark of this species is that it fails to dimerize and becomes trapped as a monomer in the absence of the active-site metals. The crystallographic data show that removal of the C57-C146 disulphide bond sets free the interface loop IV in the apo protein, whereas the same loop remains unaffected in the holo protein. Thus, the low dimerisation propensity of disulphide-reduced apoSOD seems to be of entropic origin due to increased loop flexibility in the monomeric state: in the disulphide-reduced holo protein this gain in configurational entropy upon splitting of the dimer interface is reduced by the metal coordination.
Disease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this Structure
2GBT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase., Hornberg A, Logan DT, Marklund SL, Oliveberg M, J Mol Biol. 2007 Jan 12;365(2):333-42. Epub 2006 Sep 23. PMID:17070542
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