4je6 - Revision history

OCA at 14:22, 8 November 2023

OCA — Wed, 08 Nov 2023 14:22:49 GMT

←Older revision		Revision as of 14:22, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4je6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JE6 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4je6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JE6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4je6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je6 OCA], [https://pdbe.org/4je6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4je6 RCSB], [https://www.ebi.ac.uk/pdbsum/4je6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4je6 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=4je6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je6 OCA], [https://pdbe.org/4je6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4je6 RCSB], [https://www.ebi.ac.uk/pdbsum/4je6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4je6 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 11:08, 24 November 2022

OCA — Thu, 24 Nov 2022 11:08:33 GMT

←Older revision		Revision as of 11:08, 24 November 2022
Line 1:		Line 1:

	==Crystal structure of a human-like mitochondrial peptide deformylase==		==Crystal structure of a human-like mitochondrial peptide deformylase==
-	<StructureSection load='4je6' size='340' side='right' caption='[[4je6]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4je6' size='340' side='right'caption='[[4je6]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4je6]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Arath Arath~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE6 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4JE6 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4je6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JE6 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4je7\|4je7]], [[4je8\|4je8]]</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=4je6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je6 OCA], [https://pdbe.org/4je6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4je6 RCSB], [https://www.ebi.ac.uk/pdbsum/4je6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4je6 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">At1g15390, def, DEF1, F9L1.34, F9L1_34, PDF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </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=4je6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je6 OCA], [~~http~~://pdbe.org/4je6 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4je6 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4je6 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4je6 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DEF1A_ARATH DEF1A_ARATH]] Removes the formyl group from the N-terminal Met of newly synthesized proteins.<ref>PMID:11060042</ref>	+	[https://www.uniprot.org/uniprot/DEF1A_ARATH DEF1A_ARATH] Removes the formyl group from the N-terminal Met of newly synthesized proteins.<ref>PMID:11060042</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arath~~]]	+	[[Category: Arabidopsis thaliana]]
-	[[Category: ~~Peptide deformylase~~]]	+	[[Category: Large Structures]]
-	[[Category: Fieulaine, S]]	+	[[Category: Fieulaine S]]
-	[[Category: Giglione, C]]	+	[[Category: Giglione C]]
-	[[Category: Meinnel, T]]	+	[[Category: Meinnel T]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Mitochondrial~~]]	+

OCA at 04:07, 5 August 2016

OCA — Fri, 05 Aug 2016 04:07:06 GMT

←Older revision		Revision as of 04:07, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of a human-like mitochondrial peptide deformylase==		==Crystal structure of a human-like mitochondrial peptide deformylase==
	<StructureSection load='4je6' size='340' side='right' caption='[[4je6]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4je6' size='340' side='right' caption='[[4je6]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">At1g15390, def, DEF1, F9L1.34, F9L1_34, PDF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">At1g15390, def, DEF1, F9L1.34, F9L1_34, PDF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </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=4je6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4je6 RCSB], [http://www.ebi.ac.uk/pdbsum/4je6 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=4je6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je6 OCA], [http://pdbe.org/4je6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4je6 RCSB], [http://www.ebi.ac.uk/pdbsum/4je6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4je6 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4je6" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 22:49, 24 December 2014

OCA — Wed, 24 Dec 2014 22:49:51 GMT

←Older revision		Revision as of 22:49, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4je6\| PDB=4je6 \| SCENE= }}~~	+	==Crystal structure of a human-like mitochondrial peptide deformylase==
-	===Crystal structure of a human-like mitochondrial peptide deformylase===	+	<StructureSection load='4je6' size='340' side='right' caption='[[4je6]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24531459}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4je6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JE6 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4je7\|4je7]], [[4je8\|4je8]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">At1g15390, def, DEF1, F9L1.34, F9L1_34, PDF1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </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=4je6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4je6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4je6 RCSB], [http://www.ebi.ac.uk/pdbsum/4je6 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/DEF1A_ARATH DEF1A_ARATH]] Removes the formyl group from the N-terminal Met of newly synthesized proteins.<ref>PMID:11060042</ref>		[[http://www.uniprot.org/uniprot/DEF1A_ARATH DEF1A_ARATH]] Removes the formyl group from the N-terminal Met of newly synthesized proteins.<ref>PMID:11060042</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Peptide deformylases (PDFs), which are essential and ubiquitous enzymes involved in the removal of the N-formyl group from nascent chains, are classified into four subtypes based on the structural and sequence similarity of specific conserved domains. All PDFs share a similar three-dimensional structure, are functionally interchangeable in vivo and display similar properties in vitro, indicating that their molecular mechanism has been conserved during evolution. The human mitochondrial PDF is the only exception as despite its conserved fold it reveals a unique substrate-binding pocket together with an unusual kinetic behaviour. Unlike human PDF, the closely related mitochondrial PDF1As from plants have catalytic efficiencies and enzymatic parameters that are similar to those of other classes of PDFs. Here, the aim was to identify the structural basis underlying the properties of human PDF compared with all other PDFs by focusing on plant mitochondrial PDF1A. The construction of a chimaera composed of plant PDF1A with the nonrandom substitutions found in a conserved motif of its human homologue converted it into an enzyme with properties similar to the human enzyme, indicating the crucial role of these positions. The crystal structure of this human-like plant PDF revealed that substitution of two residues leads to a reduction in the volume of the ligand-binding site together with the introduction of negative charges, unravelling the origin of the weak affinity of human PDF for its substrate. In addition, the substitution of the two residues of human PDF modifies the transition state of the reaction through alteration of the network of interactions between the catalytic residues and the substrate, leading to an overall reduced reaction rate.

-	~~==About this Structure==~~	+	Understanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpart.,Fieulaine S, Desmadril M, Meinnel T, Giglione C Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):242-52. doi:, 10.1107/S1399004713026461. Epub 2014 Jan 17. PMID:24531459<ref>PMID:24531459</ref>
-	~~[[4je6]] is a~~ 2 ~~chain structure~~. ~~Full crystallographic information is available from [http~~:/~~/oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4JE6 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024531459</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Arath]]
	[[Category: Peptide deformylase]]		[[Category: Peptide deformylase]]
-	[[Category: Fieulaine, S.]]	+	[[Category: Fieulaine, S]]
-	[[Category: Giglione, C.]]	+	[[Category: Giglione, C]]
-	[[Category: Meinnel, T.]]	+	[[Category: Meinnel, T]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Mitochondrial]]		[[Category: Mitochondrial]]
-	[[Category: Peptide deformylase]]

OCA at 06:55, 26 March 2014

OCA — Wed, 26 Mar 2014 06:55:00 GMT

←Older revision		Revision as of 06:55, 26 March 2014
Line 1:		Line 1:
	{{STRUCTURE_4je6\| PDB=4je6 \| SCENE= }}		{{STRUCTURE_4je6\| PDB=4je6 \| SCENE= }}
	===Crystal structure of a human-like mitochondrial peptide deformylase===		===Crystal structure of a human-like mitochondrial peptide deformylase===
		+	{{ABSTRACT_PUBMED_24531459}}

	==Function==		==Function==
Line 9:		Line 10:

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:024531459</ref><references group="xtra"/><references/>
	[[Category: Peptide deformylase]]		[[Category: Peptide deformylase]]
	[[Category: Fieulaine, S.]]		[[Category: Fieulaine, S.]]

OCA at 18:20, 3 March 2014

OCA — Mon, 03 Mar 2014 18:20:59 GMT

←Older revision		Revision as of 18:20, 3 March 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4je6\| PDB=4je6 \| SCENE= }}
		+	===Crystal structure of a human-like mitochondrial peptide deformylase===

-	~~The entry 4je6 is ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/DEF1A_ARATH DEF1A_ARATH]] Removes the formyl group from the N-terminal Met of newly synthesized proteins.<ref>PMID:11060042</ref>

-	~~Authors~~: ~~Fieulaine, S~~.~~, Meinnel, T~~.~~, Giglione, C~~.	+	==About this Structure==
		+	[[4je6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JE6 OCA].

-	~~Description~~: ~~Crystal structure of a human-like mitochondrial peptide~~ deformylase	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Peptide deformylase]]
		+	[[Category: Fieulaine, S.]]
		+	[[Category: Giglione, C.]]
		+	[[Category: Meinnel, T.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Mitochondrial]]
		+	[[Category: Peptide deformylase]]

OCA at 08:16, 27 March 2013

OCA — Wed, 27 Mar 2013 08:16:12 GMT

←Older revision		Revision as of 08:16, 27 March 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4je6 is ON HOLD	+	The entry 4je6 is ON HOLD until Paper Publication

	Authors: Fieulaine, S., Meinnel, T., Giglione, C.		Authors: Fieulaine, S., Meinnel, T., Giglione, C.

	Description: Crystal structure of a human-like mitochondrial peptide deformylase		Description: Crystal structure of a human-like mitochondrial peptide deformylase

OCA: Protected "4je6" [edit=sysop:move=sysop]

OCA — Wed, 06 Mar 2013 13:53:30 GMT

Protected "4je6" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:53, 6 March 2013

OCA: New page: '''Unreleased structure''' The entry 4je6 is ON HOLD Authors: Fieulaine, S., Meinnel, T., Giglione, C. Description: Crystal structure of a human-like mitochondrial peptide deformylase

OCA — Wed, 06 Mar 2013 13:53:29 GMT

New page: '''Unreleased structure''' The entry 4je6 is ON HOLD Authors: Fieulaine, S., Meinnel, T., Giglione, C. Description: Crystal structure of a human-like mitochondrial peptide deformylase

New page

'''Unreleased structure'''

The entry 4je6 is ON HOLD

Authors: Fieulaine, S., Meinnel, T., Giglione, C.

Description: Crystal structure of a human-like mitochondrial peptide deformylase