2gbt
From Proteopedia
(New page: 200px<br /> <applet load="2gbt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gbt, resolution 1.700Å" /> '''C6A/C111A CuZn Sup...) |
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| - | [[Image:2gbt. | + | [[Image:2gbt.jpg|left|200px]]<br /><applet load="2gbt" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2gbt" size=" | + | |
caption="2gbt, resolution 1.700Å" /> | caption="2gbt, resolution 1.700Å" /> | ||
'''C6A/C111A CuZn Superoxide dismutase'''<br /> | '''C6A/C111A CuZn Superoxide dismutase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GBT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CU1 and ZN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2GBT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CU1:'>CU1</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GBT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:27:42 2008'' |
Revision as of 15:27, 15 February 2008
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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 with and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 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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