This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2gbv
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2gbv.jpg|left|200px]] | [[Image:2gbv.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2gbv", 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_2gbv| PDB=2gbv | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''C6A/C111A/C57A/C146A holo CuZn Superoxide dismutase''' | '''C6A/C111A/C57A/C146A holo CuZn Superoxide dismutase''' | ||
| Line 33: | Line 30: | ||
[[Category: Marklund, S L.]] | [[Category: Marklund, S L.]] | ||
[[Category: Oliveberg, M.]] | [[Category: Oliveberg, M.]] | ||
| - | [[Category: | + | [[Category: Cystein-free]] |
| - | [[Category: | + | [[Category: Human cu/zn superoxide dismutase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:55:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:55, 4 May 2008
C6A/C111A/C57A/C146A holo 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
2GBV 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 04:55:51 2008
