5lx1 - Revision history

OCA at 18:54, 18 October 2023

OCA — Wed, 18 Oct 2023 18:54:41 GMT

←Older revision		Revision as of 18:54, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='5lx1' size='340' side='right'caption='[[5lx1]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='5lx1' size='340' side='right'caption='[[5lx1]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lx1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LX1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5LX1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lx1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LX1 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 2.7Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5lwz\|5lwz]], [[5lx0\|5lx0]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Membrane_dipeptidase Membrane dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.19 3.4.13.19]~~ </~~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=5lx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lx1 OCA], [https://pdbe.org/5lx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lx1 RCSB], [https://www.ebi.ac.uk/pdbsum/5lx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lx1 ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5lx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lx1 OCA], [~~http~~://pdbe.org/5lx1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lx1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lx1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lx1 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/GLIJ_ASPFU GLIJ_ASPFU]] Dipeptidase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).<ref>PMID:17154540</ref> <ref>PMID:18199036</ref> <ref>PMID:20548963</ref> <ref>PMID:21513890</ref> <ref>PMID:21612254</ref> <ref>PMID:21749092</ref> <ref>PMID:22903976</ref> <ref>PMID:22936680</ref> <ref>PMID:23434416</ref> <ref>PMID:24039048</ref> <ref>PMID:25062268</ref>	+	[https://www.uniprot.org/uniprot/GLIJ_ASPFU GLIJ_ASPFU] Dipeptidase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).<ref>PMID:17154540</ref> <ref>PMID:18199036</ref> <ref>PMID:20548963</ref> <ref>PMID:21513890</ref> <ref>PMID:21612254</ref> <ref>PMID:21749092</ref> <ref>PMID:22903976</ref> <ref>PMID:22936680</ref> <ref>PMID:23434416</ref> <ref>PMID:24039048</ref> <ref>PMID:25062268</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aspergillus fumigatus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Membrane dipeptidase]]~~	+	[[Category: Groll M]]
-	[[Category: Groll, M]]	+	[[Category: Huber EM]]
-	[[Category: Huber~~, E M]]~~	+
-	~~[[Category: Carboxypeptidase]]~~	+
-	~~[[Category: Dipeptidase]]~~	+
-	~~[[Category: Gliotoxin biosynthesis]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 10:53, 12 August 2020

OCA — Wed, 12 Aug 2020 10:53:09 GMT

←Older revision		Revision as of 10:53, 12 August 2020
Line 1:		Line 1:

	==Cys-Gly dipeptidase GliJ mutant D304A==		==Cys-Gly dipeptidase GliJ mutant D304A==
-	<StructureSection load='5lx1' size='340' side='right' caption='[[5lx1]], [[Resolution\|resolution]] 2.70Å' scene=''>	+	<StructureSection load='5lx1' size='340' side='right'caption='[[5lx1]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lx1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LX1 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LX1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lx1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LX1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LX1 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5lwz\|5lwz]], [[5lx0\|5lx0]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5lwz\|5lwz]], [[5lx0\|5lx0]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_dipeptidase Membrane dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.19 3.4.13.19] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_dipeptidase Membrane dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.19 3.4.13.19] </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=5lx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lx1 OCA], [http://pdbe.org/5lx1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lx1 RCSB], [http://www.ebi.ac.uk/pdbsum/5lx1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lx1 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lx1 OCA], [http://pdbe.org/5lx1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lx1 RCSB], [http://www.ebi.ac.uk/pdbsum/5lx1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lx1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Membrane dipeptidase]]		[[Category: Membrane dipeptidase]]
	[[Category: Groll, M]]		[[Category: Groll, M]]

OCA at 04:17, 4 August 2017

OCA — Fri, 04 Aug 2017 04:17:32 GMT

←Older revision		Revision as of 04:17, 4 August 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5lx1 is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Cys-Gly dipeptidase GliJ mutant D304A==
		+	<StructureSection load='5lx1' size='340' side='right' caption='[[5lx1]], [[Resolution\|resolution]] 2.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5lx1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LX1 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5lwz\|5lwz]], [[5lx0\|5lx0]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Membrane_dipeptidase Membrane dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.19 3.4.13.19] </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=5lx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lx1 OCA], [http://pdbe.org/5lx1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lx1 RCSB], [http://www.ebi.ac.uk/pdbsum/5lx1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lx1 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/GLIJ_ASPFU GLIJ_ASPFU]] Dipeptidase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP (PubMed:17154540, PubMed:21612254). GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp (PubMed:23434416). The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain (PubMed:24039048, PubMed:23434416). The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin (PubMed:21513890, PubMed:21749092). This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties (PubMed:22903976, PubMed:24039048). Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure (PubMed:20548963, PubMed:22936680, PubMed:24039048, PubMed:25062268). GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides (PubMed:25062268). Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA (PubMed:26150413). Gliotoxin contributes to pathogenesis during invasive aspergillosis (PubMed:17601876, PubMed:18199036). In macrophages and neutrophils, gliotoxin showed inhibition of various different cell functions including cytokine production, antigen presentation, phagocytosis, and production of reactive oxygen species (PubMed:17601876).<ref>PMID:17154540</ref> <ref>PMID:18199036</ref> <ref>PMID:20548963</ref> <ref>PMID:21513890</ref> <ref>PMID:21612254</ref> <ref>PMID:21749092</ref> <ref>PMID:22903976</ref> <ref>PMID:22936680</ref> <ref>PMID:23434416</ref> <ref>PMID:24039048</ref> <ref>PMID:25062268</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The formation of glutathione (GSH) conjugates, best known from the detoxification of xenobiotics, is a widespread strategy to incorporate sulfur into biomolecules. The biosynthesis of gliotoxin, a virulence factor of the human pathogenic fungus Aspergillus fumigatus, involves attachment of two GSH molecules and their sequential decomposition to yield two reactive thiol groups. The degradation of the GSH moieties requires the activity of the Cys-Gly carboxypeptidase GliJ, for which we describe the X-ray structure here. The enzyme forms a homodimer with each monomer comprising one active site. Two metal ions are present per proteolytic center, thus assigning GliJ to the diverse family of dinuclear metallohydrolases. Depending on availability, Zn2+, Fe2+, Fe3+, Mn2+, Cu2+, Co2+, or Ni2+ ions are accepted as cofactors. Despite this high metal promiscuity, a preference for zinc versus iron and manganese was noted. Mutagenesis experiments revealed details of metal coordination, and molecular modeling delivered insights into substrate recognition and processing by GliJ. The latter results suggest a reaction mechanism in which the two scissile peptide bonds of one gliotoxin precursor molecule are hydrolyzed sequentially and in a given order.

-	~~Authors~~: ~~Huber~~, ~~E.M~~., Groll, M.	+	Gliotoxin Biosynthesis: Structure, Mechanism, and Metal Promiscuity of Carboxypeptidase GliJ.,Marion A, Groll M, Scharf DH, Scherlach K, Glaser M, Sievers H, Schuster M, Hertweck C, Brakhage AA, Antes I, Huber EM ACS Chem Biol. 2017 Jul 21;12(7):1874-1882. doi: 10.1021/acschembio.6b00847. Epub, 2017 Jun 6. PMID:28525266<ref>PMID:28525266</ref>

-	~~Description: Cys~~-~~Gly dipeptidase GliJ mutant D304A~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5lx1" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Membrane dipeptidase]]
	[[Category: Groll, M]]		[[Category: Groll, M]]
-	[[Category: Huber, E.M]]	+	[[Category: Huber, E M]]
		+	[[Category: Carboxypeptidase]]
		+	[[Category: Dipeptidase]]
		+	[[Category: Gliotoxin biosynthesis]]
		+	[[Category: Hydrolase]]

OCA at 07:50, 10 May 2017

OCA — Wed, 10 May 2017 07:50:14 GMT

←Older revision		Revision as of 07:50, 10 May 2017
Line 5:		Line 5:
	Authors: Huber, E.M., Groll, M.		Authors: Huber, E.M., Groll, M.

-	Description: ~~iron-dependent~~ Cys-Gly dipeptidase GliJ mutant D304A	+	Description: Cys-Gly dipeptidase GliJ mutant D304A
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Groll, M]]		[[Category: Groll, M]]
	[[Category: Huber, E.M]]		[[Category: Huber, E.M]]

OCA at 10:55, 9 March 2017

OCA — Thu, 09 Mar 2017 10:55:53 GMT

←Older revision		Revision as of 10:55, 9 March 2017
Line 7:		Line 7:
	Description: iron-dependent Cys-Gly dipeptidase GliJ mutant D304A		Description: iron-dependent Cys-Gly dipeptidase GliJ mutant D304A
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Huber, E.M]]
	[[Category: Groll, M]]		[[Category: Groll, M]]
		+	[[Category: Huber, E.M]]

OCA: Protected "5lx1" [edit=sysop:move=sysop]

OCA — Mon, 03 Oct 2016 14:49:43 GMT

Protected "5lx1" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:49, 3 October 2016

OCA: New page: '''Unreleased structure''' The entry 5lx1 is ON HOLD until Paper Publication Authors: Huber, E.M., Groll, M. Description: iron-dependent Cys-Gly dipeptidase GliJ mutant D304A [[Categor...

OCA — Mon, 03 Oct 2016 14:49:42 GMT

New page: '''Unreleased structure''' The entry 5lx1 is ON HOLD until Paper Publication Authors: Huber, E.M., Groll, M. Description: iron-dependent Cys-Gly dipeptidase GliJ mutant D304A [[Categor...

New page

'''Unreleased structure'''

The entry 5lx1 is ON HOLD until Paper Publication

Authors: Huber, E.M., Groll, M.

Description: iron-dependent Cys-Gly dipeptidase GliJ mutant D304A
[[Category: Unreleased Structures]]
[[Category: Huber, E.M]]
[[Category: Groll, M]]