8dsj - Revision history

OCA at 10:13, 25 October 2023

2023-10-25T10:13:59Z

← Older revision		Revision as of 10:13, 25 October 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8dsj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DSJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[8dsj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DSJ 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.8Å</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=GOL:GLYCEROL'>GOL</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=8dsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dsj OCA], [https://pdbe.org/8dsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dsj RCSB], [https://www.ebi.ac.uk/pdbsum/8dsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dsj 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=8dsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dsj OCA], [https://pdbe.org/8dsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dsj RCSB], [https://www.ebi.ac.uk/pdbsum/8dsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dsj ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:23, 22 March 2023

2023-03-22T07:23:40Z

← Older revision		Revision as of 07:23, 22 March 2023
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	~~'''Unreleased structure'''~~

	The ~~entry 8dsj~~ is ~~ON HOLD until Paper~~ Publication		==Peptidylglycine alpha hydroxylating monooxygenase anaerobic==
			<StructureSection load='8dsj' size='340' side='right'caption='[[8dsj]], [[Resolution\|resolution]] 2.80Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[8dsj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DSJ 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=8dsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dsj OCA], [https://pdbe.org/8dsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dsj RCSB], [https://www.ebi.ac.uk/pdbsum/8dsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dsj ProSAT]</span></td></tr>
			</table>
			== Function ==
			[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Peptidylglycine monooxygenase (PHM) is essential for the biosynthesis of many neuroendocrine peptides via a copper-dependent hydroxylation of a glycine-extended pro-peptide. The "canonical" mechanism requires the transfer of two electrons from one mononuclear copper (CuH, H-site) to a second mononuclear copper (CuM, M-site) which is the site of oxygen binding and catalysis. In most crystal structures the copper centers are separated by 11 A of disordered solvent, but recent work has established that a PHM variant H108A forms a closed conformer in the presence of citrate with a reduced Cu-Cu site separation of ~4 A. Here we report three new PHM structures where the H and M sites are separated by a longer distance of ~14 A. Variation in Cu-Cu distance is the result of a rotation of the M subdomain about a hinge point centered on the pro(199) -leu(200) -ile(201) triad which forms the linker between subdomains. The energetic cost of domain dynamics is likely small enough to allow free rotation of the subdomains relative to each other, adding credence to recent suggestions that an open-to-closed transition to form a binuclear oxygen binding intermediate is an essential element of catalysis. This inference would explain many experimental observations that are inconsistent with the current canonical mechanism including substrate-induced oxygen activation and isotope scrambling during the peroxide shunt. This article is protected by copyright. All rights reserved.

	~~Authors:~~ Arias, R.J.~~, Blackburn, N~~.J.		New Structures Reveal Flexible Dynamics between the Subdomains of Peptidylglycine Monooxygenase. Implications for an Open to Closed Mechanism.,Arias RJ, Welch EF, Blackburn NJ Protein Sci. 2023 Mar 7:e4615. doi: 10.1002/pro.4615. PMID:36880254<ref>PMID:36880254</ref>

	~~Description~~: ~~Peptidylglycine alpha hydroxylating monooxygenase anaerobic~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	[[Category: ~~Unreleased~~ Structures]]		</div>
	[[Category: Arias~~, R.J~~]]		<div class="pdbe-citations 8dsj" style="background-color:#fffaf0;"></div>
	[[Category: Blackburn~~, N.J~~]]		== References ==
			<references/>
			__TOC__
			</StructureSection>
			[[Category: Large Structures]]
			[[Category: Rattus norvegicus]]
			[[Category: Arias RJ]]
			[[Category: Blackburn NJ]]

OCA at 05:31, 31 August 2022

2022-08-31T05:31:24Z

← Older revision		Revision as of 05:31, 31 August 2022
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 8dsj is ON HOLD		The entry 8dsj is ON HOLD until Paper Publication

	Authors: Arias, R.J., Blackburn, N.J.		Authors: Arias, R.J., Blackburn, N.J.

OCA: Protected "8dsj" [edit=sysop:move=sysop]

2022-08-03T03:55:11Z

Protected "8dsj" [edit=sysop:move=sysop]

← Older revision	Revision as of 03:55, 3 August 2022
(No difference)

OCA: New page: '''Unreleased structure''' The entry 8dsj is ON HOLD Authors: Arias, R.J., Blackburn, N.J. Description: Peptidylglycine alpha hydroxylating monooxygenase anaerobic [[Category: Unreleas...

2022-08-03T03:55:10Z

New page: '''Unreleased structure''' The entry 8dsj is ON HOLD Authors: Arias, R.J., Blackburn, N.J. Description: Peptidylglycine alpha hydroxylating monooxygenase anaerobic [[Category: Unreleas...

New page

'''Unreleased structure'''

The entry 8dsj is ON HOLD

Authors: Arias, R.J., Blackburn, N.J.

Description: Peptidylglycine alpha hydroxylating monooxygenase anaerobic
[[Category: Unreleased Structures]]
[[Category: Arias, R.J]]
[[Category: Blackburn, N.J]]