1uv2: Difference between revisions
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[[ | ==HADDOCK MODEL OF THE COMPLEX BETWEEN THE COPPER CHAPERONE ATX1 AND THE ATPASE CCC2 FROM YEAST== | ||
<StructureSection load='1uv2' size='340' side='right'caption='[[1uv2]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UV2 FirstGlance]. <br> | |||
</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=1uv2 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1uv2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uv2 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A structural model of the transient complex between the yeast copper chaperone Atx1 and the first soluble domain of the copper transporting ATPase Ccc2 was obtained with HADDOCK, combining NMR chemical shift mapping information with in silico docking. These two proteins are involved in copper trafficking in yeast cells. Calculations were performed starting with the copper ion either bound to Atx1 or to Ccc2 and using the experimental structures of the copper-loaded and apo forms of each protein. The copper binding motifs of the two proteins are found in close proximity. Copper tends to move from Atx1 to Ccc2, consistent with the physiological direction of transfer, with concomitant structural rearrangements, in agreement with experimental observations. The interaction is mainly of an electrostatic nature with hydrogen bonds stabilizing the complex. The structural data are relevant for a number of proteins homologous to Atx1 and Ccc2 and conserved from bacteria to humans. | |||
A docking approach to the study of copper trafficking proteins; interaction between metallochaperones and soluble domains of copper ATPases.,Arnesano F, Banci L, Bertini I, Bonvin AM Structure. 2004 Apr;12(4):669-76. PMID:15062089<ref>PMID:15062089</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1uv2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Arnesano, F]] | [[Category: Arnesano, F]] | ||
[[Category: Banci, L]] | [[Category: Banci, L]] | ||
[[Category: Bertini, I]] | [[Category: Bertini, I]] | ||
[[Category: Bonvin, A M.J J]] | [[Category: Bonvin, A M.J J]] | ||
Latest revision as of 09:18, 6 October 2021
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HADDOCK MODEL OF THE COMPLEX BETWEEN THE COPPER CHAPERONE ATX1 AND THE ATPASE CCC2 FROM YEASTHADDOCK MODEL OF THE COMPLEX BETWEEN THE COPPER CHAPERONE ATX1 AND THE ATPASE CCC2 FROM YEAST
Structural highlights
Publication Abstract from PubMedA structural model of the transient complex between the yeast copper chaperone Atx1 and the first soluble domain of the copper transporting ATPase Ccc2 was obtained with HADDOCK, combining NMR chemical shift mapping information with in silico docking. These two proteins are involved in copper trafficking in yeast cells. Calculations were performed starting with the copper ion either bound to Atx1 or to Ccc2 and using the experimental structures of the copper-loaded and apo forms of each protein. The copper binding motifs of the two proteins are found in close proximity. Copper tends to move from Atx1 to Ccc2, consistent with the physiological direction of transfer, with concomitant structural rearrangements, in agreement with experimental observations. The interaction is mainly of an electrostatic nature with hydrogen bonds stabilizing the complex. The structural data are relevant for a number of proteins homologous to Atx1 and Ccc2 and conserved from bacteria to humans. A docking approach to the study of copper trafficking proteins; interaction between metallochaperones and soluble domains of copper ATPases.,Arnesano F, Banci L, Bertini I, Bonvin AM Structure. 2004 Apr;12(4):669-76. PMID:15062089[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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