1fvq: Difference between revisions

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-[[Image:1fvq.png|left|200px]]
-<!--
+==SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES==
-The line below this paragraph, containing "STRUCTURE_1fvq", creates the "Structure Box" on the page.
+<StructureSection load='1fvq' size='340' side='right'caption='[[1fvq]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1fvq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FVQ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1fvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fvq OCA], [https://pdbe.org/1fvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fvq RCSB], [https://www.ebi.ac.uk/pdbsum/1fvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fvq ProSAT]</span></td></tr>
-{{STRUCTURE_1fvq|  PDB=1fvq  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATU2_YEAST ATU2_YEAST] Probably involved in copper transport and in the regulation of cellular copper level. Retrieves copper from the metallochaperone ATX1 and incorporates it into trans-Golgi vesicles.
+== 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/fv/1fvq_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=1fvq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ccc2 is an intracellular copper transporter in Saccharomyces cerevisiae and is a physiological target of the copper chaperone Atx1. Here we describe the solution structure of the first N-terminal MTCXXC metal-binding domain, Ccc2a, both in the presence and absence of Cu(I). For Cu(I)-Ccc2a, 1944 meaningful nuclear Overhauser effects were used to obtain a family of 35 structures with root mean square deviation to the average structure of 0.36 +/- 0.06 A for the backbone and 0.79 +/- 0.05 A for the heavy atoms. For apo-Ccc2a, 1970 meaningful nuclear Overhauser effects have been used with 35 (3)J(HNHalpha) to obtain a family of 35 structures with root mean square deviation to the average structure of 0.38 +/- 0.06 A for the backbone and 0.82 +/- 0.07 A for the heavy atoms. The protein exhibits a betaalphabetabetaalphabeta, ferrodoxin-like fold similar to that of its target Atx1 and that of a human counterpart, the fourth metal-binding domain of the Menkes protein. The overall fold remains unchanged upon copper loading, but the copper-binding site itself becomes less disordered. The helical context of the copper-binding site, and the copper-induced conformational changes in Ccc2a differ from those in Atx1. Ccc2a presents a conserved acidic surface which complements the basic surface of Atx1 and a hydrophobic surface. These results open new mechanistic aspects of copper transporter domains with physiological copper donor and acceptor proteins.
-===SOLUTION STRUCTURE OF THE YEAST COPPER TRANSPORTER DOMAIN CCC2A IN THE APO AND CU(I) LOADED STATES===
+Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states.,Banci L, Bertini I, Ciofi-Baffoni S, Huffman DL, O'Halloran TV J Biol Chem. 2001 Mar 16;276(11):8415-26. Epub 2000 Nov 16. PMID:11083871<ref>PMID:11083871</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11083871}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1fvq" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11083871 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_11083871}}
-==About this Structure==
-[[1fvq]] is a 1 chain structure of [[ATPase]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FVQ OCA].
 ==See Also==
-*[[ATPase]]
+*[[ATPase 3D structures|ATPase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:11083871</ref><references group="xtra"/>
+__TOC__
-[[Category: Hydrogen/potassium-exchanging ATPase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Baffoni, S Ciofi.]]
+[[Category: Banci L]]
-[[Category: Banci, L.]]
+[[Category: Bertini I]]
-[[Category: Bertini, I.]]
+[[Category: Ciofi Baffoni S]]
-[[Category: Halloran, T V.O.]]
+[[Category: Huffman DL]]
-[[Category: Huffman, D L.]]
+[[Category: O'Halloran TV]]
-[[Category: Apo-ccc2a]]
-[[Category: Hydrolase]]