2xmu: Difference between revisions
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==Copper chaperone Atx1 from Synechocystis PCC6803 (Cu2 form)== | |||
===COPPER | <StructureSection load='2xmu' size='340' side='right' caption='[[2xmu]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
{{ | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xmu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XMU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XMU FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sb6|1sb6]], [[2xmt|2xmt]], [[2xmm|2xmm]], [[2xmk|2xmk]], [[2xmj|2xmj]], [[2xmv|2xmv]], [[2xmw|2xmw]]</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=2xmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xmu RCSB], [http://www.ebi.ac.uk/pdbsum/2xmu 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/xm/2xmu_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Molecular systems have evolved to permit the safe delivery of copper. Despite extensive studies, many copper site structures involved in copper homeostasis, even for the well-studied metallochaperone Atx1, remain unresolved. Cyanobacteria import copper to their thylakoid compartments for use in photosynthesis and respiration and possess an Atx1 that we show can adopt multiple oligomeric states when metalated, capable of binding up to four copper ions. Two-copper- and four-copper-loaded dimers exist in solution at low micromolar concentrations, and head-to-head and side-to-side arrangements, respectively, can be crystallized, with the latter binding a [Cu(4){mu(2)-S(gamma)(Cys)}(4)Cl(2)](2-) cluster. The His61Tyr mutation on loop 5 weakens head-to-head dimerization, yet a side-to-side dimer binding a similar cluster as in the wild-type protein, but with phenolate coordination, is present. The cognate metal-binding domains (MBDs) of the P-type ATPases CtaA and PacS, which are proposed to donate copper to and accept copper from Atx1, respectively, are monomeric in the presence of copper. The structure of the MBD of Cu(I)-PacS shows a crystallographic trimer arrangement around a [Cu(3){mu(2)-S(gamma)(Cys)}(3){S(gamma)(Cys)}(3)](2-) cluster that is very similar to that found for an alternate form of the His61Tyr Atx1 mutant. Copper transfer from the MBD of CtaA to Atx1 is favorable, but delivery from Atx1 to the MBD of PacS is strongly dependent upon the dimeric form of Atx1. A copper-induced switch in Atx1 dimer structure may have a regulatory role with cluster formation helping to buffer copper. | |||
Visualizing the metal-binding versatility of copper trafficking sites .,Badarau A, Firbank SJ, McCarthy AA, Banfield MJ, Dennison C Biochemistry. 2010 Sep 14;49(36):7798-810. PMID:20726513<ref>PMID:20726513</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
[[Category: Badarau, A | <references/> | ||
[[Category: Banfield, M J | __TOC__ | ||
[[Category: Dennison, C | </StructureSection> | ||
[[Category: Firbank, S J | [[Category: Badarau, A]] | ||
[[Category: | [[Category: Banfield, M J]] | ||
[[Category: Dennison, C]] | |||
[[Category: Firbank, S J]] | |||
[[Category: McCarthy, A A]] | |||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Copper homeostasis]] | [[Category: Copper homeostasis]] | ||