1hl5: Difference between revisions

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[[Image:1hl5.gif|left|200px]]
[[Image:1hl5.gif|left|200px]]


{{Structure
<!--
|PDB= 1hl5 |SIZE=350|CAPTION= <scene name='initialview01'>1hl5</scene>, resolution 1.80&Aring;
The line below this paragraph, containing "STRUCTURE_1hl5", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+S'>AC1</scene>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|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>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1hl5| PDB=1hl5  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl5 OCA], [http://www.ebi.ac.uk/pdbsum/1hl5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hl5 RCSB]</span>
}}


'''THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE'''
'''THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE'''
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[[Category: Strange, R W.]]
[[Category: Strange, R W.]]
[[Category: Valentine, J S.]]
[[Category: Valentine, J S.]]
[[Category: acetylation]]
[[Category: Acetylation]]
[[Category: amyotrophic lateral sclerosis]]
[[Category: Amyotrophic lateral sclerosis]]
[[Category: antioxidant]]
[[Category: Antioxidant]]
[[Category: copper]]
[[Category: Copper]]
[[Category: disease mutation]]
[[Category: Disease mutation]]
[[Category: human cu]]
[[Category: Human cu]]
[[Category: metal-binding]]
[[Category: Metal-binding]]
[[Category: oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: zinc]]
[[Category: Zinc]]
[[Category: zn superoxide dismutase]]
[[Category: Zn superoxide dismutase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:58:15 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:07:04 2008''

Revision as of 18:58, 2 May 2008

File:1hl5.gif

Template:STRUCTURE 1hl5

THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE


OverviewOverview

Cu, Zn superoxide dismutase (SOD1) forms a crucial component of the cellular defence against oxidative stress. Zn-deficient wild-type and mutant human SOD1 have been implicated in the disease familial amyotrophic lateral sclerosis (FALS). We present here the crystal structures of holo and metal-deficient (apo) wild-type protein at 1.8A resolution. The P21 wild-type holo enzyme structure has nine independently refined dimers and these combine to form a "trimer of dimers" packing motif in each asymmetric unit. There is no significant asymmetry between the monomers in these dimers, in contrast to the subunit structures of the FALS G37R mutant of human SOD1 and in bovine Cu,Zn SOD. Metal-deficient apo SOD1 crystallizes with two dimers in the asymmetric unit and shows changes in the metal-binding sites and disorder in the Zn binding and electrostatic loops of one dimer, which is devoid of metals. The second dimer lacks Cu but has approximately 20% occupancy of the Zn site and remains structurally similar to wild-type SOD1. The apo protein forms a continuous, extended arrangement of beta-barrels stacked up along the short crystallographic b-axis, while perpendicular to this axis, the constituent beta-strands form a zig-zag array of filaments, the overall arrangement of which has a similarity to the common structure associated with amyloid-like fibrils.

About this StructureAbout this Structure

1HL5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis., Strange RW, Antonyuk S, Hough MA, Doucette PA, Rodriguez JA, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS, J Mol Biol. 2003 May 9;328(4):877-91. PMID:12729761 Page seeded by OCA on Fri May 2 18:58:15 2008

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