View source for 1hl4

==THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE==
<StructureSection load='1hl4' size='340' side='right' caption='[[1hl4]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hl4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HL4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HL4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wz6|2wz6]], [[1oez|1oez]], [[1ptz|1ptz]], [[1azv|1azv]], [[2wyz|2wyz]], [[1ozu|1ozu]], [[2vr6|2vr6]], [[2c9v|2c9v]], [[2wz5|2wz5]], [[2xjl|2xjl]], [[1pu0|1pu0]], [[1fun|1fun]], [[2xjk|2xjk]], [[1sos|1sos]], [[1n19|1n19]], [[1p1v|1p1v]], [[1l3n|1l3n]], [[2wko|2wko]], [[2wz0|2wz0]], [[1uxl|1uxl]], [[2af2|2af2]], [[2vr8|2vr8]], [[1rk7|1rk7]], [[2vr7|2vr7]], [[2v0a|2v0a]], [[1mfm|1mfm]], [[2c9s|2c9s]], [[4sod|4sod]], [[2wyt|2wyt]], [[1dsw|1dsw]], [[1kmg|1kmg]], [[1ozt|1ozt]], [[1n18|1n18]], [[1ba9|1ba9]], [[1hl5|1hl5]], [[2c9u|2c9u]], [[1uxm|1uxm]], [[1spd|1spd]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hl4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hl4 OCA], [http://pdbe.org/1hl4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hl4 RCSB], [http://www.ebi.ac.uk/pdbsum/1hl4 PDBsum]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/1hl4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hl4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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<ref>PMID:12729761</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1hl4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Superoxide Dismutase|Superoxide Dismutase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Superoxide dismutase]]
[[Category: Antonyuk, S]]
[[Category: Doucette, P]]
[[Category: Hart, P J]]
[[Category: Hasnain, S S]]
[[Category: Hayward, L J]]
[[Category: Hough, M A]]
[[Category: Rodriguez, J]]
[[Category: Strange, R W]]
[[Category: Valentine, J S]]
[[Category: Human cu]]
[[Category: Oxidoreductase]]
[[Category: Zn superoxide dismutase]]