6p1e - Revision history

OCA at 14:53, 13 March 2024

2024-03-13T14:53:43Z

←Older revision		Revision as of 14:53, 13 March 2024
Line 3:		Line 3:
	<StructureSection load='6p1e' size='340' side='right'caption='[[6p1e]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='6p1e' size='340' side='right'caption='[[6p1e]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6p1e]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Methylocystis_sp.~~_atcc_49242~~ Methylocystis sp. ~~atcc~~ 49242]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P1E OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6P1E FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6p1e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylocystis_sp._ATCC_49242 Methylocystis sp. ATCC 49242]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P1E 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>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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]] 1.605Å</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=6p1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p1e OCA], [~~http~~://pdbe.org/6p1e PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6p1e RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6p1e PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6p1e ProSAT]</span></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>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=6p1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p1e OCA], [https://pdbe.org/6p1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p1e RCSB], [https://www.ebi.ac.uk/pdbsum/6p1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p1e ProSAT]</span></td></tr>
	</table>		</table>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Copper is critically important for methanotrophic bacteria because their primary metabolic enzyme, particulate methane monooxygenase (pMMO), is copper-dependent. In addition to pMMO, many other copper proteins are encoded in the genomes of methanotrophs, including proteins that contain periplasmic copper-A chaperone (PCuAC) domains. Using bioinformatics analyses, we identified three distinct classes of PCuAC domain-containing proteins in methanotrophs, termed PmoF1, PmoF2, and PmoF3. PCuAC domains from other types of bacteria bind a single Cu(I) ion via an HxnMx21/22HxM motif, which is also present in PmoF3, but PmoF1 and PmoF2 lack this motif entirely. Instead, the PCuAC domains of PmoF1 and PmoF2 bind only Cu(II), and PmoF1 binds additional Cu(II) ions in a His-rich extension to its PCuAC domain. Crystal structures of the PmoF1 and PmoF2 PCuAC domains reveal that Cu(II) is coordinated by an N-terminal histidine brace Hx10H motif. This binding site is distinct from those of previously characterized PCuAC domains, but resembles copper centers in CopC proteins and lytic polysaccharide monooxygenase (LPMO) enzymes. Bioinformatics analysis of the entire PCuAC family revealed previously unappreciated diversity, including sequences that contain both the HxnMx21/22HxMand Hx10H motifs, and sequences that lack either set of copper-binding ligands. These findings provide the first characterization of an additional class of copper proteins from methanotrophs, further expand the PCuAC family, and afford new insight into the biological significance of histidine brace-mediated copper coordination.
-
-	PCuAC domains from methane-oxidizing bacteria use a histidine brace to bind copper.,Fisher OS, Sendzik MR, Ross MO, Lawton TJ, Hoffman BM, Rosenzweig AC J Biol Chem. 2019 Sep 16. pii: RA119.010093. doi: 10.1074/jbc.RA119.010093. PMID:31527086<ref>PMID:31527086</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 6p1e" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Methylocystis sp. ~~atcc~~ 49242]]	+	[[Category: Methylocystis sp. ATCC 49242]]
-	[[Category: Fisher~~, O S~~]]	+	[[Category: Fisher OS]]
-	[[Category: Rosenzweig~~, A C~~]]	+	[[Category: Rosenzweig AC]]
-	[[Category: Sendzik~~, M R]]~~	+	[[Category: Sendzik MR]]
-	~~[[Category: Chaperone]]~~	+
-	~~[[Category: Copper binding protein]]~~	+
-	~~[[Category: Metal binding protein~~]]	+

OCA at 11:17, 2 October 2019

2019-10-02T11:17:12Z

←Older revision		Revision as of 11:17, 2 October 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6p1e is ~~ON HOLD~~	+	==Cu-bound PmoF1 PCuAC domain (dimer)==
		+	<StructureSection load='6p1e' size='340' side='right'caption='[[6p1e]], [[Resolution\|resolution]] 1.60Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6p1e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylocystis_sp._atcc_49242 Methylocystis sp. atcc 49242]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P1E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P1E 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>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></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=6p1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p1e OCA], [http://pdbe.org/6p1e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p1e RCSB], [http://www.ebi.ac.uk/pdbsum/6p1e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p1e ProSAT]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Copper is critically important for methanotrophic bacteria because their primary metabolic enzyme, particulate methane monooxygenase (pMMO), is copper-dependent. In addition to pMMO, many other copper proteins are encoded in the genomes of methanotrophs, including proteins that contain periplasmic copper-A chaperone (PCuAC) domains. Using bioinformatics analyses, we identified three distinct classes of PCuAC domain-containing proteins in methanotrophs, termed PmoF1, PmoF2, and PmoF3. PCuAC domains from other types of bacteria bind a single Cu(I) ion via an HxnMx21/22HxM motif, which is also present in PmoF3, but PmoF1 and PmoF2 lack this motif entirely. Instead, the PCuAC domains of PmoF1 and PmoF2 bind only Cu(II), and PmoF1 binds additional Cu(II) ions in a His-rich extension to its PCuAC domain. Crystal structures of the PmoF1 and PmoF2 PCuAC domains reveal that Cu(II) is coordinated by an N-terminal histidine brace Hx10H motif. This binding site is distinct from those of previously characterized PCuAC domains, but resembles copper centers in CopC proteins and lytic polysaccharide monooxygenase (LPMO) enzymes. Bioinformatics analysis of the entire PCuAC family revealed previously unappreciated diversity, including sequences that contain both the HxnMx21/22HxMand Hx10H motifs, and sequences that lack either set of copper-binding ligands. These findings provide the first characterization of an additional class of copper proteins from methanotrophs, further expand the PCuAC family, and afford new insight into the biological significance of histidine brace-mediated copper coordination.

-	~~Authors~~:	+	PCuAC domains from methane-oxidizing bacteria use a histidine brace to bind copper.,Fisher OS, Sendzik MR, Ross MO, Lawton TJ, Hoffman BM, Rosenzweig AC J Biol Chem. 2019 Sep 16. pii: RA119.010093. doi: 10.1074/jbc.RA119.010093. PMID:31527086<ref>PMID:31527086</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 6p1e" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Methylocystis sp. atcc 49242]]
		+	[[Category: Fisher, O S]]
		+	[[Category: Rosenzweig, A C]]
		+	[[Category: Sendzik, M R]]
		+	[[Category: Chaperone]]
		+	[[Category: Copper binding protein]]
		+	[[Category: Metal binding protein]]

OCA: Protected "6p1e" [edit=sysop:move=sysop]

2019-05-29T04:35:17Z

Protected "6p1e" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:35, 29 May 2019

OCA: New page: '''Unreleased structure''' The entry 6p1e is ON HOLD Authors: Description: Category: Unreleased Structures

2019-05-29T04:35:15Z

New page: '''Unreleased structure''' The entry 6p1e is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6p1e is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]