1fd8 - Revision history

OCA at 08:28, 22 May 2024

OCA — Wed, 22 May 2024 08:28:30 GMT

←Older revision		Revision as of 08:28, 22 May 2024
Line 20:		Line 20:
	</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=1fd8 ConSurf].		</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=1fd8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The (1)H NMR solution structure of the Cu(I)-bound form of Atx1, a 73-amino acid metallochaperone protein from the yeast Saccharomyces cerevisiae, has been determined. Ninety percent of the (1)H and 95% of the (15)N resonances were assigned, and 1184 meaningful NOEs and 42 (3)J(HNH)(alpha) and 60 (1)J(HN) residual dipolar couplings provided a family of structures with rmsd values to the mean structure of 0.37 +/- 0.07 A for the backbone and 0.83 +/- 0.08 A for all heavy atoms. The structure is constituted by four antiparallel beta strands and two alpha helices in a betaalphabetabetaalphabeta fold. Following EXAFS data [Pufahl, R., Singer, C. P., Peariso, K. L., Lin, S.-J., Schmidt, P. J., Fahrni, C. J., Cizewski Culotta, V., Penner-Hahn, J. E., and O'Halloran, T. V. (1997) Science 278, 853-856], a copper ion can be placed between two sulfur atoms of Cys15 and Cys18. The structure of the reduced apo form has also been determined with similar resolution using 1252 meaningful NOEs (rmsd values for the family to the mean structure are 0.67 +/- 0.12 A for the backbone and 1.00 +/- 0.12 A for all heavy atoms). Comparison of the Cu(I) and apo conformations of the protein reveals that the Cu(I) binding cysteines move from a buried site in the bound metal form to a solvent-exposed conformation on the surface of the protein after copper release. Furthermore, copper release leads to a less helical character in the metal binding site. Comparison with the Hg(II)-Atx1 solid-state structure [Rosenzweig, A. C., Huffman, D. L., Hou, M. Y., Wernimont, A. K., Pufahl, R. A., and O'Halloran, T. V. (1999) Structure 7, 605-617] provides insights into the copper transfer mechanism, and a pivotal role for Lys65 in the metal capture and release process is proposed.
		+
		+	Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1.,Arnesano F, Banci L, Bertini I, Huffman DL, O'Halloran TV Biochemistry. 2001 Feb 13;40(6):1528-39. PMID:11327811<ref>PMID:11327811</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 1fd8" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:13, 20 March 2024

OCA — Wed, 20 Mar 2024 10:13:48 GMT

←Older revision		Revision as of 10:13, 20 March 2024
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1==		==SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1==
-	<StructureSection load='1fd8' size='340' side='right'caption='[[1fd8~~]], [[NMR_Ensembles_of_Models \| 1 NMR models~~]]' scene=''>	+	<StructureSection load='1fd8' size='340' side='right'caption='[[1fd8]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_18824 Atcc 18824~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fd8]] 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=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>~~</td></tr>	+	</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1cc8\|1cc8]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [https://pdbe.org/1fd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [https://www.ebi.ac.uk/pdbsum/1fd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd8 ProSAT]</span></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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [https://pdbe.org/1fd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [https://www.ebi.ac.uk/pdbsum/1fd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST]] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.	+	[https://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</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=1fd8 ConSurf].		</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=1fd8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The (1)H NMR solution structure of the Cu(I)-bound form of Atx1, a 73-amino acid metallochaperone protein from the yeast Saccharomyces cerevisiae, has been determined. Ninety percent of the (1)H and 95% of the (15)N resonances were assigned, and 1184 meaningful NOEs and 42 (3)J(HNH)(alpha) and 60 (1)J(HN) residual dipolar couplings provided a family of structures with rmsd values to the mean structure of 0.37 +/- 0.07 A for the backbone and 0.83 +/- 0.08 A for all heavy atoms. The structure is constituted by four antiparallel beta strands and two alpha helices in a betaalphabetabetaalphabeta fold. Following EXAFS data [Pufahl, R., Singer, C. P., Peariso, K. L., Lin, S.-J., Schmidt, P. J., Fahrni, C. J., Cizewski Culotta, V., Penner-Hahn, J. E., and O'Halloran, T. V. (1997) Science 278, 853-856], a copper ion can be placed between two sulfur atoms of Cys15 and Cys18. The structure of the reduced apo form has also been determined with similar resolution using 1252 meaningful NOEs (rmsd values for the family to the mean structure are 0.67 +/- 0.12 A for the backbone and 1.00 +/- 0.12 A for all heavy atoms). Comparison of the Cu(I) and apo conformations of the protein reveals that the Cu(I) binding cysteines move from a buried site in the bound metal form to a solvent-exposed conformation on the surface of the protein after copper release. Furthermore, copper release leads to a less helical character in the metal binding site. Comparison with the Hg(II)-Atx1 solid-state structure [Rosenzweig, A. C., Huffman, D. L., Hou, M. Y., Wernimont, A. K., Pufahl, R. A., and O'Halloran, T. V. (1999) Structure 7, 605-617] provides insights into the copper transfer mechanism, and a pivotal role for Lys65 in the metal capture and release process is proposed.
-
-	Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1.,Arnesano F, Banci L, Bertini I, Huffman DL, O'Halloran TV Biochemistry. 2001 Feb 13;40(6):1528-39. PMID:11327811<ref>PMID:11327811</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1fd8" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 18824]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Arnesano, F~~]]	+	[[Category: Saccharomyces cerevisiae]]
-	[[Category: ~~Banci, L~~]]	+	[[Category: Arnesano F]]
-	[[Category: ~~Bertini, I~~]]	+	[[Category: Banci L]]
-	[[Category: ~~Halloran, T V.O~~]]	+	[[Category: Bertini I]]
-	[[Category: Huffman~~, D L~~]]	+	[[Category: Huffman DL]]
-	[[Category: ~~Atx1]]~~	+	[[Category: O'Halloran TV]]
-	~~[[Category: Heavy-metal-associated domain]]~~	+
-	~~[[Category: Metal transport]]~~	+
-	~~[[Category: Metallochaperone]]~~	+
-	~~[[Category: Oxygen toxicity~~]]	+

OCA at 07:46, 23 February 2022

OCA — Wed, 23 Feb 2022 07:46:24 GMT

←Older revision		Revision as of 07:46, 23 February 2022
Line 3:		Line 3:
	<StructureSection load='1fd8' size='340' side='right'caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1fd8' size='340' side='right'caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[1cc8\|1cc8]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cc8\|1cc8]]</div></td></tr>
Line 33:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Atcc 18824]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Arnesano, F]]		[[Category: Arnesano, F]]

OCA at 07:03, 24 March 2021

OCA — Wed, 24 Mar 2021 07:03:26 GMT

←Older revision		Revision as of 07:03, 24 March 2021
Line 3:		Line 3:
	<StructureSection load='1fd8' size='340' side='right'caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1fd8' size='340' side='right'caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FD8 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>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">[[1cc8\|1cc8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cc8\|1cc8]]</div></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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [~~http~~://pdbe.org/1fd8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1fd8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd8 ProSAT]</span></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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [https://pdbe.org/1fd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [https://www.ebi.ac.uk/pdbsum/1fd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST]] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.	+	[[https://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST]] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:38, 19 June 2019

OCA — Wed, 19 Jun 2019 07:38:48 GMT

←Older revision		Revision as of 07:38, 19 June 2019
Line 1:		Line 1:

	==SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1==		==SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1==
-	<StructureSection load='1fd8' size='340' side='right' caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>	+	<StructureSection load='1fd8' size='340' side='right'caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fd8_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fd/1fd8_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Arnesano, F]]		[[Category: Arnesano, F]]
	[[Category: Banci, L]]		[[Category: Banci, L]]

OCA at 10:59, 13 September 2017

OCA — Wed, 13 Sep 2017 10:59:57 GMT

←Older revision		Revision as of 10:59, 13 September 2017
Line 1:		Line 1:
		+
	==SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1==		==SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1==
	<StructureSection load='1fd8' size='340' side='right' caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1fd8' size='340' side='right' caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure ~~with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]~~. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 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>		</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">[[1cc8\|1cc8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1cc8\|1cc8]]</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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://pdbe.org/1fd8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum]</span></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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://pdbe.org/1fd8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</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].	+	</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=1fd8 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 32:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 18824]]
	[[Category: Arnesano, F]]		[[Category: Arnesano, F]]
	[[Category: Banci, L]]		[[Category: Banci, L]]

OCA at 10:22, 11 September 2015

OCA — Fri, 11 Sep 2015 10:22:05 GMT

←Older revision		Revision as of 10:22, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1fd8' size='340' side='right' caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>		<StructureSection load='1fd8' size='340' side='right' caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure 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=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 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>		</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">[[1cc8\|1cc8]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1cc8\|1cc8]]</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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum]</span></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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://pdbe.org/1fd8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 27:		Line 27:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1fd8" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae~~]]	+	[[Category: Atcc 18824]]
	[[Category: Arnesano, F]]		[[Category: Arnesano, F]]
	[[Category: Banci, L]]		[[Category: Banci, L]]

OCA at 15:08, 25 December 2014

OCA — Thu, 25 Dec 2014 15:08:04 GMT

←Older revision		Revision as of 15:08, 25 December 2014
Line 7:		Line 7:
	<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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum]</span></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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ATX1_YEAST ATX1_YEAST]] Shuttles copper to the transport ATPase CCC2. Protects against oxygen toxicity.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 00:47, 23 December 2014

OCA — Tue, 23 Dec 2014 00:47:51 GMT

←Older revision		Revision as of 00:47, 23 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure 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=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure 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=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene><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><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1cc8\|1cc8]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1cc8\|1cc8]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum]</span></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=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
-	[[Category: Arnesano, F.]]	+	[[Category: Arnesano, F]]
-	[[Category: Banci, L.]]	+	[[Category: Banci, L]]
-	[[Category: Bertini, I.]]	+	[[Category: Bertini, I]]
-	[[Category: Halloran, T V.O.]]	+	[[Category: Halloran, T V.O]]
-	[[Category: Huffman, D L.]]	+	[[Category: Huffman, D L]]
	[[Category: Atx1]]		[[Category: Atx1]]
	[[Category: Heavy-metal-associated domain]]		[[Category: Heavy-metal-associated domain]]

OCA at 14:39, 28 September 2014

OCA — Sun, 28 Sep 2014 14:39:29 GMT

←Older revision		Revision as of 14:39, 28 September 2014
Line 1:		Line 1:
-	[[~~Image:~~1fd8.~~png~~\|~~left~~\|200px]]	+	==SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE, ATX1==
		+	<StructureSection load='1fd8' size='340' side='right' caption='[[1fd8]], [[NMR_Ensembles_of_Models \| 1 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1fd8]] is a 1 chain structure 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=1FD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FD8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1cc8\|1cc8]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fd8 RCSB], [http://www.ebi.ac.uk/pdbsum/1fd8 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/fd/1fd8_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 ==
		+	The (1)H NMR solution structure of the Cu(I)-bound form of Atx1, a 73-amino acid metallochaperone protein from the yeast Saccharomyces cerevisiae, has been determined. Ninety percent of the (1)H and 95% of the (15)N resonances were assigned, and 1184 meaningful NOEs and 42 (3)J(HNH)(alpha) and 60 (1)J(HN) residual dipolar couplings provided a family of structures with rmsd values to the mean structure of 0.37 +/- 0.07 A for the backbone and 0.83 +/- 0.08 A for all heavy atoms. The structure is constituted by four antiparallel beta strands and two alpha helices in a betaalphabetabetaalphabeta fold. Following EXAFS data [Pufahl, R., Singer, C. P., Peariso, K. L., Lin, S.-J., Schmidt, P. J., Fahrni, C. J., Cizewski Culotta, V., Penner-Hahn, J. E., and O'Halloran, T. V. (1997) Science 278, 853-856], a copper ion can be placed between two sulfur atoms of Cys15 and Cys18. The structure of the reduced apo form has also been determined with similar resolution using 1252 meaningful NOEs (rmsd values for the family to the mean structure are 0.67 +/- 0.12 A for the backbone and 1.00 +/- 0.12 A for all heavy atoms). Comparison of the Cu(I) and apo conformations of the protein reveals that the Cu(I) binding cysteines move from a buried site in the bound metal form to a solvent-exposed conformation on the surface of the protein after copper release. Furthermore, copper release leads to a less helical character in the metal binding site. Comparison with the Hg(II)-Atx1 solid-state structure [Rosenzweig, A. C., Huffman, D. L., Hou, M. Y., Wernimont, A. K., Pufahl, R. A., and O'Halloran, T. V. (1999) Structure 7, 605-617] provides insights into the copper transfer mechanism, and a pivotal role for Lys65 in the metal capture and release process is proposed.

-	~~{{STRUCTURE_1fd8\| PDB=1fd8 \| SCENE= }}~~	+	Solution structure of the Cu(I) and apo forms of the yeast metallochaperone, Atx1.,Arnesano F, Banci L, Bertini I, Huffman DL, O'Halloran TV Biochemistry. 2001 Feb 13;40(6):1528-39. PMID:11327811<ref>PMID:11327811</ref>

-	~~===SOLUTION STRUCTURE OF THE CU(I) FORM OF THE YEAST METALLOCHAPERONE~~, ~~ATX1===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~==About this Structure==~~	+	<references/>
-	~~[[1fd8]] is~~ a ~~1 chain structure 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=1FD8 OCA].~~	+	__TOC__
-		+	</StructureSection>
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:011327811<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Saccharomyces cerevisiae]]		[[Category: Saccharomyces cerevisiae]]
	[[Category: Arnesano, F.]]		[[Category: Arnesano, F.]]