2gbt

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[[Image:2gbt.jpg|left|200px]]
[[Image:2gbt.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2gbt |SIZE=350|CAPTION= <scene name='initialview01'>2gbt</scene>, resolution 1.700&Aring;
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The line below this paragraph, containing "STRUCTURE_2gbt", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= SOD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_2gbt| PDB=2gbt | SCENE= }}
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|RELATEDENTRY=[[1hl4|1HL4]], [[2gbu|2GBU]], [[2gbv|2GBV]]
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|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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}}
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'''C6A/C111A CuZn Superoxide dismutase'''
'''C6A/C111A CuZn Superoxide dismutase'''
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[[Category: Marklund, S L.]]
[[Category: Marklund, S L.]]
[[Category: Oliveberg, M.]]
[[Category: Oliveberg, M.]]
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[[Category: human cu/zn superoxide dismutase]]
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[[Category: Human cu/zn superoxide dismutase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:55:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:14:33 2008''
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Revision as of 01:55, 4 May 2008

Image:2gbt.jpg

Template:STRUCTURE 2gbt

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

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