2gbt
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2gbt.jpg|left|200px]] | [[Image:2gbt.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2gbt", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_2gbt| PDB=2gbt | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''C6A/C111A CuZn Superoxide dismutase''' | '''C6A/C111A CuZn Superoxide dismutase''' | ||
Line 33: | Line 30: | ||
[[Category: Marklund, S L.]] | [[Category: Marklund, S L.]] | ||
[[Category: Oliveberg, M.]] | [[Category: Oliveberg, M.]] | ||
- | [[Category: | + | [[Category: Human cu/zn superoxide dismutase]] |
- | [[Category: | + | [[Category: Oxidoreductase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:55:35 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 01:55, 4 May 2008
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 Page seeded by OCA on Sun May 4 04:55:35 2008