2gb2 - Revision history

OCA at 09:27, 14 February 2024

2024-02-14T09:27:01Z

←Older revision		Revision as of 09:27, 14 February 2024
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	<StructureSection load='2gb2' size='340' side='right'caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>		<StructureSection load='2gb2' size='340' side='right'caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_17741 Atcc 17741~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.25Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~mauC, ami ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode~~=~~Info&srchmode~~=~~5&id=266 ATCC 17741]~~)</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [https://pdbe.org/2gb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2gb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gb2 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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [https://pdbe.org/2gb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2gb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gb2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.	+	[https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
	== 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=2gb2 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=2gb2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Amicyanin is a type I copper protein that is the natural electron acceptor for the quinoprotein methylamine dehydrogenase (MADH). The conversion of Proline52 of amicyanin to a glycine does not alter the physical and spectroscopic properties of the copper binding site, but it does alter the rate of electron transfer (ET) from MADH. The values of electronic coupling (H(AB)) and reorganization energy (lambda) that are associated with the true ET reaction from the reduced O-quinol tryptophan tryptophylquinone (TTQ) of MADH to oxidized amicyanin are significantly altered as a consequence of the P52G mutation. The experimentally determined H(AB) increases from 12 to 78 cm(-1), and lambda increases from 2.3 to 2.8 eV. The rate and salt-dependence of the proton transfer-gated ET reaction from N-quinol MADH to amicyanin are also changed by the P52G mutation. Kinetic data suggests that a new common reaction step has become rate-limiting for both the true and gated ET reactions that occur from different redox forms of MADH. A comparison of the crystal structures of P52G amicyanin with those of native amicyanin free and in complex with MADH provided clues as to the basis for the change in ET parameters. The mutation results in the loss of three carbons from Pro52 and the movement of the neighboring residue Met51. This reduces the number of hydrophobic interactions with MADH in the complex and perturbs the protein-protein interface. A model is proposed for the ET reaction with P52G amicyanin in which the most stable conformation of the protein-protein complex with MADH is not optimal for ET. A new preceding kinetic step is introduced prior to true ET that requires P52G amicyanin to switch from this redox-inactive stable complex to a redox-active unstable complex. Thus, the ET reaction of P52G amicyanin is no longer a true ET but one that is conformationally gated by the reorientation of the proteins within the ET protein complex. This same reaction step now also gates the ET from N-quinol MADH, which is normally rate-limited by a proton transfer.

-	Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated.,Ma JK, Carrell CJ, Mathews FS, Davidson VL Biochemistry. 2006 Jul 11;45(27):8284-93. PMID:16819827<ref>PMID:16819827</ref>	+	==See Also==
-		+	*[[Amicyanin 3D structures\|Amicyanin 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 2gb2" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 17741]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Carrell, C J~~]]	+	[[Category: Paracoccus denitrificans]]
-	[[Category: ~~Davidson, V L~~]]	+	[[Category: Carrell CJ]]
-	[[Category: ~~Ma, J K~~]]	+	[[Category: Davidson VL]]
-	[[Category: ~~Mathews, F S~~]]	+	[[Category: Ma JK]]
-	[[Category: ~~Beta-sandwich]]~~	+	[[Category: Mathews FS]]
-	~~[[Category: Electron transport~~]]	+

OCA at 18:54, 10 March 2021

2021-03-10T18:54:49Z

←Older revision		Revision as of 18:54, 10 March 2021
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	==The P52G mutant of amicyanin in the Cu(II) state.==		==The P52G mutant of amicyanin in the Cu(II) state.==
-	<StructureSection load='2gb2' size='340' side='right' caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>	+	<StructureSection load='2gb2' size='340' side='right'caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [~~http~~://pdbe.org/2gb2 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2gb2 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2gb2 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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [https://pdbe.org/2gb2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [https://www.ebi.ac.uk/pdbsum/2gb2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gb2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.	+	[[https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/2gb2_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/2gb2_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 34:		Line 34:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 17741]]		[[Category: Atcc 17741]]
		+	[[Category: Large Structures]]
	[[Category: Carrell, C J]]		[[Category: Carrell, C J]]
	[[Category: Davidson, V L]]		[[Category: Davidson, V L]]

OCA at 07:53, 18 October 2017

2017-10-18T07:53:17Z

←Older revision		Revision as of 07:53, 18 October 2017
Line 1:		Line 1:
		+
	==The P52G mutant of amicyanin in the Cu(II) state.==		==The P52G mutant of amicyanin in the Cu(II) state.==
	<StructureSection load='2gb2' size='340' side='right' caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>		<StructureSection load='2gb2' size='340' side='right' caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [http://pdbe.org/2gb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gb2 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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [http://pdbe.org/2gb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gb2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gb2 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 22:03, 9 February 2016

2016-02-09T22:03:29Z

←Older revision		Revision as of 22:03, 9 February 2016
Line 17:		Line 17:
	<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=2gb2 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 02:27, 11 September 2015

2015-09-11T02:27:49Z

←Older revision		Revision as of 02:27, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2gb2' size='340' side='right' caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>		<StructureSection load='2gb2' size='340' side='right' caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Paracoccus_denitrificans Paracoccus denitrificans~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ~~Paracoccus denitrificans~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741])</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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gb2 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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [http://pdbe.org/2gb2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gb2 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 2gb2" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Paracoccus denitrificans~~]]	+	[[Category: Atcc 17741]]
	[[Category: Carrell, C J]]		[[Category: Carrell, C J]]
	[[Category: Davidson, V L]]		[[Category: Davidson, V L]]

OCA at 09:50, 25 December 2014

2014-12-25T09:50:18Z

←Older revision		Revision as of 09:50, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 Paracoccus denitrificans])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 Paracoccus denitrificans])</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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gb2 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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gb2 PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 30:		Line 32:
	</StructureSection>		</StructureSection>
	[[Category: Paracoccus denitrificans]]		[[Category: Paracoccus denitrificans]]
-	[[Category: Carrell, C J.]]	+	[[Category: Carrell, C J]]
-	[[Category: Davidson, V L.]]	+	[[Category: Davidson, V L]]
-	[[Category: Ma, J K.]]	+	[[Category: Ma, J K]]
-	[[Category: Mathews, F S.]]	+	[[Category: Mathews, F S]]
	[[Category: Beta-sandwich]]		[[Category: Beta-sandwich]]
	[[Category: Electron transport]]		[[Category: Electron transport]]

OCA at 08:39, 30 September 2014

2014-09-30T08:39:01Z

←Older revision		Revision as of 08:39, 30 September 2014
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-	[[~~Image:~~2gb2.~~png~~\|~~left~~\|200px]]	+	==The P52G mutant of amicyanin in the Cu(II) state.==
		+	<StructureSection load='2gb2' size='340' side='right' caption='[[2gb2]], [[Resolution\|resolution]] 1.25Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2gb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GB2 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauC, ami ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 Paracoccus denitrificans])</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=2gb2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gb2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gb2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gb2 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/gb/2gb2_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 ==
		+	Amicyanin is a type I copper protein that is the natural electron acceptor for the quinoprotein methylamine dehydrogenase (MADH). The conversion of Proline52 of amicyanin to a glycine does not alter the physical and spectroscopic properties of the copper binding site, but it does alter the rate of electron transfer (ET) from MADH. The values of electronic coupling (H(AB)) and reorganization energy (lambda) that are associated with the true ET reaction from the reduced O-quinol tryptophan tryptophylquinone (TTQ) of MADH to oxidized amicyanin are significantly altered as a consequence of the P52G mutation. The experimentally determined H(AB) increases from 12 to 78 cm(-1), and lambda increases from 2.3 to 2.8 eV. The rate and salt-dependence of the proton transfer-gated ET reaction from N-quinol MADH to amicyanin are also changed by the P52G mutation. Kinetic data suggests that a new common reaction step has become rate-limiting for both the true and gated ET reactions that occur from different redox forms of MADH. A comparison of the crystal structures of P52G amicyanin with those of native amicyanin free and in complex with MADH provided clues as to the basis for the change in ET parameters. The mutation results in the loss of three carbons from Pro52 and the movement of the neighboring residue Met51. This reduces the number of hydrophobic interactions with MADH in the complex and perturbs the protein-protein interface. A model is proposed for the ET reaction with P52G amicyanin in which the most stable conformation of the protein-protein complex with MADH is not optimal for ET. A new preceding kinetic step is introduced prior to true ET that requires P52G amicyanin to switch from this redox-inactive stable complex to a redox-active unstable complex. Thus, the ET reaction of P52G amicyanin is no longer a true ET but one that is conformationally gated by the reorientation of the proteins within the ET protein complex. This same reaction step now also gates the ET from N-quinol MADH, which is normally rate-limited by a proton transfer.

-	~~{{STRUCTURE_2gb2\| PDB=2gb2 \| SCENE= }}~~	+	Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated.,Ma JK, Carrell CJ, Mathews FS, Davidson VL Biochemistry. 2006 Jul 11;45(27):8284-93. PMID:16819827<ref>PMID:16819827</ref>

-	~~===The P52G mutant~~ of ~~amicyanin in~~ the ~~Cu(II) state~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_16819827}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[2gb2]] is a 1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/~~wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:016819827<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Paracoccus denitrificans]]		[[Category: Paracoccus denitrificans]]
	[[Category: Carrell, C J.]]		[[Category: Carrell, C J.]]

OCA: Protected "2gb2" [edit=sysop:move=sysop]

2013-01-07T13:37:55Z

Protected "2gb2" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:37, 7 January 2013

OCA at 13:37, 7 January 2013

2013-01-07T13:37:52Z

←Older revision		Revision as of 13:37, 7 January 2013
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-	{{Seed}}
	[[Image:2gb2.png\|left\|200px]]		[[Image:2gb2.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2gb2\| PDB=2gb2 \| SCENE= }}		{{STRUCTURE_2gb2\| PDB=2gb2 \| SCENE= }}

	===The P52G mutant of amicyanin in the Cu(II) state.===		===The P52G mutant of amicyanin in the Cu(II) state.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_16819827}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 16819827 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_16819827}}		{{ABSTRACT_PUBMED_16819827}}

	==About this Structure==		==About this Structure==
-	~~2GB2~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA].	+	[[2gb2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~16819827~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:016819827</ref><references group="xtra"/>
	[[Category: Paracoccus denitrificans]]		[[Category: Paracoccus denitrificans]]
	[[Category: Carrell, C J.]]		[[Category: Carrell, C J.]]
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	[[Category: Mathews, F S.]]		[[Category: Mathews, F S.]]
	[[Category: Beta-sandwich]]		[[Category: Beta-sandwich]]
-		+	[[Category: Electron transport]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 13:05:28 2009''~~	+

OCA at 11:05, 17 February 2009

2009-02-17T11:05:30Z

←Older revision		Revision as of 11:05, 17 February 2009
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	==About this Structure==		==About this Structure==
-	2GB2 is a ~~[[Single protein]]~~ structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA].	+	2GB2 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GB2 OCA].

	==Reference==		==Reference==
-	Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated., Ma JK, Carrell CJ, Mathews FS, Davidson VL, Biochemistry. 2006 Jul 11;45(27):8284-93. PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/16819827 16819827]~~	+	<ref group="xtra">PMID:16819827</ref><references group="xtra"/>
	[[Category: Paracoccus denitrificans]]		[[Category: Paracoccus denitrificans]]
-	[[Category: Single protein]]
	[[Category: Carrell, C J.]]		[[Category: Carrell, C J.]]
	[[Category: Davidson, V L.]]		[[Category: Davidson, V L.]]
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	[[Category: Beta-sandwich]]		[[Category: Beta-sandwich]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Mon Jul 28~~ 17:35:~~00 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:05:28 2009''