2qif

<StructureSection load='2qif' size='340' side='right' caption='[[2qif]], [[Resolution|resolution]] 1.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[2qif]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QIF FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">copZ, yvgY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</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=2qif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qif OCA], [http://pdbe.org/2qif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qif RCSB], [http://www.ebi.ac.uk/pdbsum/2qif PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/COPZ_BACSU COPZ_BACSU]] Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase CopA.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qi/2qif_consurf.spt"</scriptWhenChecked>

</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].

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== Publication Abstract from PubMed ==

Copper trafficking proteins and copper-sensitive regulators are often found to be able to bind multiple Cu(I) ions in the form of Cu(I) clusters. We have determined the high-resolution X-ray crystal structure of an Atx1-like copper chaperone protein from Bacillus subtilis containing a novel tetranuclear Cu(I) cluster. The identities and oxidation states of the cluster ions were established unambiguously by refinement of X-ray energy-dependent anomalous scattering factors. The [Cu(4)(S-Cys)(4)(N-His)(2)] cluster geometry provides new structural insights into not only the binding of multiple cuprous ions by metallochaperones but also protein-associated tetranuclear Cu(I) clusters, including those found in eukaryotic copper-responsive transcription factors.

A tetranuclear Cu(I) cluster in the metallochaperone protein CopZ.,Hearnshaw S, West C, Singleton C, Zhou L, Kihlken MA, Strange RW, Le Brun NE, Hemmings AM Biochemistry. 2009 Oct 13;48(40):9324-6. PMID:19746989<ref>PMID:19746989</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2qif" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Brun, N E.Le]]

[[Category: Hemmings, A M]]

[[Category: Kihlken, M A]]

[[Category: Singleton, C]]

[[Category: West, C]]

[[Category: Chaperone]]