2hu9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="2hu9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hu9, resolution 1.780Å" /> '''X-ray structure of ...
 
OCA (talk | contribs)
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2hu9.jpg|left|200px]]<br /><applet load="2hu9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hu9, resolution 1.780&Aring;" />
'''X-ray structure of the Archaeoglobus fulgidus CopZ N-terminal Domain'''<br />


==Overview==
==X-ray structure of the Archaeoglobus fulgidus CopZ N-terminal Domain==
Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are, homologous to the human Wilson and Menkes disease proteins. The genome of, the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper, chaperone that contains an unusual cysteine-rich N-terminal domain of 130, amino acids in addition to a C-terminal copper binding domain with a, conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to, proteins found only in extremophiles and is the only such protein that is, fused to a copper chaperone. Surprisingly, optical, electron paramagnetic, resonance, and x-ray absorption spectroscopic data indicate the presence, of a [2Fe-2S] cluster in CopZ-NT. The intact CopZ protein binds two copper, ions, one in each domain. The 1.8 A resolution crystal structure of, CopZ-NT reveals that the [2Fe-2S] cluster is housed within a novel fold, and that the protein also binds a zinc ion at a four-cysteine site. CopZ, can deliver Cu+ to the A. fulgidus CopA N-terminal metal binding domain, and is capable of reducing Cu2+ to Cu+. This unique fusion of a, redox-active domain with a CXXC-containing copper chaperone domain is, relevant to the evolution of copper homeostatic mechanisms and suggests, new models for copper trafficking.
<StructureSection load='2hu9' size='340' side='right'caption='[[2hu9]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hu9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HU9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hu9 OCA], [https://pdbe.org/2hu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hu9 RCSB], [https://www.ebi.ac.uk/pdbsum/2hu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hu9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COPZ_ARCFU COPZ_ARCFU] Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) directly to the transmembrane transport sites of copper-exporting P-type ATPase A (CopA). Probably has a redox function due to the presence of a 2Fe-2S cluster and could reduce Cu(2+) to Cu(+).<ref>PMID:17609202</ref> <ref>PMID:18417453</ref>
== 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/hu/2hu9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2hu9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial CopZ proteins deliver copper to P1B-type Cu+-ATPases that are homologous to the human Wilson and Menkes disease proteins. The genome of the hyperthermophile Archaeoglobus fulgidus encodes a putative CopZ copper chaperone that contains an unusual cysteine-rich N-terminal domain of 130 amino acids in addition to a C-terminal copper binding domain with a conserved CXXC motif. The N-terminal domain (CopZ-NT) is homologous to proteins found only in extremophiles and is the only such protein that is fused to a copper chaperone. Surprisingly, optical, electron paramagnetic resonance, and x-ray absorption spectroscopic data indicate the presence of a [2Fe-2S] cluster in CopZ-NT. The intact CopZ protein binds two copper ions, one in each domain. The 1.8 A resolution crystal structure of CopZ-NT reveals that the [2Fe-2S] cluster is housed within a novel fold and that the protein also binds a zinc ion at a four-cysteine site. CopZ can deliver Cu+ to the A. fulgidus CopA N-terminal metal binding domain and is capable of reducing Cu2+ to Cu+. This unique fusion of a redox-active domain with a CXXC-containing copper chaperone domain is relevant to the evolution of copper homeostatic mechanisms and suggests new models for copper trafficking.


==About this Structure==
Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus.,Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ, Stemmler TL, Hoffman BM, Arguello JM, Rosenzweig AC J Biol Chem. 2007 Aug 31;282(35):25950-9. Epub 2007 Jul 3. PMID:17609202<ref>PMID:17609202</ref>
2HU9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HU9 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus., Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ, Stemmler TL, Hoffman BM, Arguello JM, Rosenzweig AC, J Biol Chem. 2007 Aug 31;282(35):25950-9. Epub 2007 Jul 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17609202 17609202]
</div>
<div class="pdbe-citations 2hu9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arguello, J.M.]]
[[Category: Arguello JM]]
[[Category: LeMoine, B.]]
[[Category: LeMoine B]]
[[Category: Rosenzweig, A.C.]]
[[Category: Rosenzweig AC]]
[[Category: Sazinsky, M.H.]]
[[Category: Sazinsky MH]]
[[Category: ACY]]
[[Category: FES]]
[[Category: ZN]]
[[Category: atox1]]
[[Category: atx1]]
[[Category: copper chaperone]]
[[Category: copz]]
[[Category: iron-sufur protein]]
[[Category: metal transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:48:54 2008''