7kz7 - Revision history

OCA at 15:34, 18 October 2023

OCA — Wed, 18 Oct 2023 15:34:57 GMT

←Older revision		Revision as of 15:34, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='7kz7' size='340' side='right'caption='[[7kz7]], [[Resolution\|resolution]] 1.80Å' scene=''>		<StructureSection load='7kz7' size='340' side='right'caption='[[7kz7]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7kz7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KZ7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7kz7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KZ7 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EDO:1,2~~-~~ETHANEDIOL'>EDO</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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]] 1.8Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>CBB2_0680 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~1491~~ "~~Bacillus botulinus~~" ~~van Ermengem 1896])~~<~~/td~~></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69]~~ </~~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=7kz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kz7 OCA], [https://pdbe.org/7kz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kz7 RCSB], [https://www.ebi.ac.uk/pdbsum/7kz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kz7 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=7kz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kz7 OCA], [https://pdbe.org/7kz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kz7 RCSB], [https://www.ebi.ac.uk/pdbsum/7kz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kz7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BXX_CLOBO BXX_CLOBO]] Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin X which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). Artificially assembled BoNT/X cleaves synaptobrevin-2/VAMP2 and VAMP4 in cultured rat neurons and causes flaccid paralysis in mice (PubMed:28770820).[UniProtKB:P0DPI0]<ref>PMID:28770820</ref> Has proteolytic activity. After translocation into the eukaryotic host cytosol, LC hydrolyzes the '66-Arg-\|-Ala-67' bond in synaptobrevin-2/VAMP2, and the equivalent bonds in 'Arg-\|-Ala' bonds in VAMP1 and VAMP3, thus blocking neurotransmitter release (PubMed:28770820). Has a wider target range than most BoNTs, as it also cleaves the '87-Arg-\|-Ser-89' bond in VAMP4, the '40-Arg-\|-Ser-41' bond in VAMP5 and the '173-Lys-\|-Ser-174' bond in YKT6; whether these are physiologically relevant substrates is unknown (PubMed:28770820). BoNT/X is 10-fold more efficient than BoNT/B and 40-fold more efficient than TeTX on an artificial human VAMP1 substrate (PubMed:29540745).<ref>PMID:28770820</ref> <ref>PMID:29540745</ref> Responsible for epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and an unknown receptor protein in close proximity on host synaptic vesicles. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity). Protein ligation of the RBD to the rest of the toxin (creates an artificial whole toxin) greatly increases VAMP2 degradation, and thus neuron uptake (PubMed:28770820).[UniProtKB:P10844]<ref>PMID:28770820</ref>	+	[https://www.uniprot.org/uniprot/BXX_CLOBO BXX_CLOBO] Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin X which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). Artificially assembled BoNT/X cleaves synaptobrevin-2/VAMP2 and VAMP4 in cultured rat neurons and causes flaccid paralysis in mice (PubMed:28770820).[UniProtKB:P0DPI0]<ref>PMID:28770820</ref> Has proteolytic activity. After translocation into the eukaryotic host cytosol, LC hydrolyzes the '66-Arg-\|-Ala-67' bond in synaptobrevin-2/VAMP2, and the equivalent bonds in 'Arg-\|-Ala' bonds in VAMP1 and VAMP3, thus blocking neurotransmitter release (PubMed:28770820). Has a wider target range than most BoNTs, as it also cleaves the '87-Arg-\|-Ser-89' bond in VAMP4, the '40-Arg-\|-Ser-41' bond in VAMP5 and the '173-Lys-\|-Ser-174' bond in YKT6; whether these are physiologically relevant substrates is unknown (PubMed:28770820). BoNT/X is 10-fold more efficient than BoNT/B and 40-fold more efficient than TeTX on an artificial human VAMP1 substrate (PubMed:29540745).<ref>PMID:28770820</ref> <ref>PMID:29540745</ref> Responsible for epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and an unknown receptor protein in close proximity on host synaptic vesicles. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity). Protein ligation of the RBD to the rest of the toxin (creates an artificial whole toxin) greatly increases VAMP2 degradation, and thus neuron uptake (PubMed:28770820).[UniProtKB:P10844]<ref>PMID:28770820</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus botulinus van ermengem 1896]]~~	+	[[Category: Clostridium botulinum]]
-	~~[[Category: Bontoxilysin~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Blum~~, T R]]~~	+	[[Category: Blum TR]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Dong M]]
-	[[Category: Dong, M]]	+	[[Category: Lee PG]]
-	[[Category: Lee~~, P G~~]]	+	[[Category: Liu DR]]
-	[[Category: Liu~~, D R~~]]	+	[[Category: Liu H]]
-	[[Category: Liu, H]]	+	[[Category: Minasov G]]
-	[[Category: Minasov, G]]	+	[[Category: Packer MS]]
-	[[Category: Packer~~, M S~~]]	+	[[Category: Richter M]]
-	[[Category: Richter, M]]	+	[[Category: Satchell KJF]]
-	[[Category: Satchell~~, K J.F~~]]	+	[[Category: Xiong X]]
-	[[Category: Xiong, X]]	+	[[Category: Zhang S]]
-	[[Category: Zhang, S]]	+
-	~~[[Category: Csgid]]~~	+
-	~~[[Category: Neurotoxin x]]~~	+
-	~~[[Category: Protease domain]]~~	+
-	~~[[Category: Toxin~~]]	+

OCA at 16:57, 15 December 2021

OCA — Wed, 15 Dec 2021 16:57:29 GMT

←Older revision		Revision as of 16:57, 15 December 2021
Line 1:		Line 1:

	==Crystals Structure of the Mutated Protease Domain of Botulinum Neurotoxin X (X4130B1).==		==Crystals Structure of the Mutated Protease Domain of Botulinum Neurotoxin X (X4130B1).==
-	<StructureSection load='7kz7' size='340' side='right'caption='[[7kz7]]' scene=''>	+	<StructureSection load='7kz7' size='340' side='right'caption='[[7kz7]], [[Resolution\|resolution]] 1.80Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KZ7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=7KZ7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7kz7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KZ7 FirstGlance]. <br>
-	</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=7kz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kz7 OCA], [~~http~~://pdbe.org/7kz7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=7kz7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/7kz7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=7kz7 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CBB2_0680 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </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=7kz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kz7 OCA], [https://pdbe.org/7kz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kz7 RCSB], [https://www.ebi.ac.uk/pdbsum/7kz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kz7 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/BXX_CLOBO BXX_CLOBO]] Botulinum toxin causes flaccid paralysis by inhibiting neurotransmitter (acetylcholine) release from the presynaptic membranes of nerve terminals of eukaryotic host skeletal and autonomic nervous system, with frequent heart or respiratory failure. Precursor of botulinum neurotoxin X which has 2 coreceptors; complex polysialylated gangliosides found on neural tissue and specific membrane-anchored proteins found in synaptic vesicles. Receptor proteins are exposed on host presynaptic cell membrane during neurotransmitter release, when the toxin heavy chain (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken up via the endocytic pathway. When the pH of the toxin-containing endosome drops a structural rearrangement occurs so that the N-terminus of HC forms pores that allows the light chain (LC) to translocate into the cytosol. Once in the cytosol the disulfide bond linking the 2 subunits is reduced and LC cleaves its target protein on synaptic vesicles, preventing their fusion with the cytoplasmic membrane and thus neurotransmitter release (By similarity). Artificially assembled BoNT/X cleaves synaptobrevin-2/VAMP2 and VAMP4 in cultured rat neurons and causes flaccid paralysis in mice (PubMed:28770820).[UniProtKB:P0DPI0]<ref>PMID:28770820</ref> Has proteolytic activity. After translocation into the eukaryotic host cytosol, LC hydrolyzes the '66-Arg-\|-Ala-67' bond in synaptobrevin-2/VAMP2, and the equivalent bonds in 'Arg-\|-Ala' bonds in VAMP1 and VAMP3, thus blocking neurotransmitter release (PubMed:28770820). Has a wider target range than most BoNTs, as it also cleaves the '87-Arg-\|-Ser-89' bond in VAMP4, the '40-Arg-\|-Ser-41' bond in VAMP5 and the '173-Lys-\|-Ser-174' bond in YKT6; whether these are physiologically relevant substrates is unknown (PubMed:28770820). BoNT/X is 10-fold more efficient than BoNT/B and 40-fold more efficient than TeTX on an artificial human VAMP1 substrate (PubMed:29540745).<ref>PMID:28770820</ref> <ref>PMID:29540745</ref> Responsible for epithelial cell transcytosis, host nerve cell targeting and translocation of light chain (LC) into host cytosol. Composed of 3 subdomains; the translocation domain (TD), and N-terminus and C-terminus of the receptor-binding domain (RBD). The RBD is responsible for the adherence of the toxin to the cell surface. It simultaneously recognizes 2 coreceptors; polysialated gangliosides and an unknown receptor protein in close proximity on host synaptic vesicles. The N-terminus of the TD wraps an extended belt around the perimeter of the LC, protecting Zn(2+) in the active site (By similarity). The TD inserts into synaptic vesicle membrane to allow translocation into the host cytosol (By similarity). Protein ligation of the RBD to the rest of the toxin (creates an artificial whole toxin) greatly increases VAMP2 degradation, and thus neuron uptake (PubMed:28770820).[UniProtKB:P10844]<ref>PMID:28770820</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Although bespoke, sequence-specific proteases have the potential to advance biotechnology and medicine, generation of proteases with tailor-made cleavage specificities remains a major challenge. We developed a phage-assisted protease evolution system with simultaneous positive and negative selection and applied it to three botulinum neurotoxin (BoNT) light-chain proteases. We evolved BoNT/X protease into separate variants that preferentially cleave vesicle-associated membrane protein 4 (VAMP4) and Ykt6, evolved BoNT/F protease to selectively cleave the non-native substrate VAMP7, and evolved BoNT/E protease to cleave phosphatase and tensin homolog (PTEN) but not any natural BoNT protease substrate in neurons. The evolved proteases display large changes in specificity (218- to >11,000,000-fold) and can retain their ability to form holotoxins that self-deliver into primary neurons. These findings establish a versatile platform for reprogramming proteases to selectively cleave new targets of therapeutic interest.
		+
		+	Phage-assisted evolution of botulinum neurotoxin proteases with reprogrammed specificity.,Blum TR, Liu H, Packer MS, Xiong X, Lee PG, Zhang S, Richter M, Minasov G, Satchell KJF, Dong M, Liu DR Science. 2021 Feb 19;371(6531):803-810. doi: 10.1126/science.abf5972. PMID:33602850<ref>PMID:33602850</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7kz7" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Botulinum neurotoxin 3D structures\|Botulinum neurotoxin 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Bacillus botulinus van ermengem 1896]]
		+	[[Category: Bontoxilysin]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Blum TR]]	+	[[Category: Blum, T R]]
-	[[Category: Dong M]]	+	[[Category: Structural genomic]]
-	[[Category: Lee PG]]	+	[[Category: Dong, M]]
-	[[Category: Liu DR]]	+	[[Category: Lee, P G]]
-	[[Category: Liu H]]	+	[[Category: Liu, D R]]
-	[[Category: Minasov G]]	+	[[Category: Liu, H]]
-	[[Category: Packer MS]]	+	[[Category: Minasov, G]]
-	[[Category: Richter M]]	+	[[Category: Packer, M S]]
-	[[Category: Satchell ~~KJF~~]]	+	[[Category: Richter, M]]
-	[[Category: Xiong X]]	+	[[Category: Satchell, K J.F]]
-	[[Category: Zhang S]]	+	[[Category: Xiong, X]]
		+	[[Category: Zhang, S]]
		+	[[Category: Csgid]]
		+	[[Category: Neurotoxin x]]
		+	[[Category: Protease domain]]
		+	[[Category: Toxin]]

OCA at 10:42, 24 December 2020

OCA — Thu, 24 Dec 2020 10:42:27 GMT

←Older revision		Revision as of 10:42, 24 December 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7kz7 ~~is ON HOLD~~	+	==Crystals Structure of the Mutated Protease Domain of Botulinum Neurotoxin X (X4130B1).==
-		+	<StructureSection load='7kz7' size='340' side='right'caption='[[7kz7]]' scene=''>
-	~~Authors~~: ~~Blum, T~~.R.~~, Liu, H~~.~~, Packer, M~~.S.~~, Xiong, X~~.~~, Lee, P~~.G.~~, Zhang, S~~., ~~Richter, M~~., ~~Minasov, G~~., ~~Satchell, K~~.J.F., ~~Dong, M~~., ~~Liu, D~~.R.~~, Center for Structural Genomics of Infectious Diseases (CSGID)~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KZ7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7KZ7 FirstGlance]. <br>
-	~~Description: Crystals Structure of the Mutated Protease Domain of Botulinum Neurotoxin X (X4130B1).~~	+	</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=7kz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kz7 OCA], [http://pdbe.org/7kz7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7kz7 RCSB], [http://www.ebi.ac.uk/pdbsum/7kz7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7kz7 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Dong, M~~]]	+	__TOC__
-	[[Category: ~~Satchell, K.J.F~~]]	+	</StructureSection>
-	[[Category: ~~Minasov, G~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Zhang, S]]~~	+	[[Category: Blum TR]]
-	~~[[Category: Blum, T.R~~]]	+	[[Category: Dong M]]
-	[[Category: Liu~~, D.R~~]]	+	[[Category: Lee PG]]
-	[[Category: ~~Xiong, X~~]]	+	[[Category: Liu DR]]
-	[[Category: Packer~~, M.S~~]]	+	[[Category: Liu H]]
-	[[Category: ~~Liu, H~~]]	+	[[Category: Minasov G]]
-	[[Category: ~~Center For Structural Genomics Of Infectious Diseases (Csgid)~~]]	+	[[Category: Packer MS]]
-	[[Category: ~~Richter, M~~]]	+	[[Category: Richter M]]
-	[[Category: ~~Lee, P.G~~]]	+	[[Category: Satchell KJF]]
		+	[[Category: Xiong X]]
		+	[[Category: Zhang S]]

OCA: Protected "7kz7" [edit=sysop:move=sysop]

OCA — Wed, 16 Dec 2020 11:17:04 GMT

Protected "7kz7" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:17, 16 December 2020

OCA: New page: '''Unreleased structure''' The entry 7kz7 is ON HOLD Authors: Blum, T.R., Liu, H., Packer, M.S., Xiong, X., Lee, P.G., Zhang, S., Richter, M., Minasov, G., Satchell, K.J.F., Dong, M., L...

OCA — Wed, 16 Dec 2020 11:17:03 GMT

New page: '''Unreleased structure''' The entry 7kz7 is ON HOLD Authors: Blum, T.R., Liu, H., Packer, M.S., Xiong, X., Lee, P.G., Zhang, S., Richter, M., Minasov, G., Satchell, K.J.F., Dong, M., L...

New page

'''Unreleased structure'''

The entry 7kz7 is ON HOLD

Authors: Blum, T.R., Liu, H., Packer, M.S., Xiong, X., Lee, P.G., Zhang, S., Richter, M., Minasov, G., Satchell, K.J.F., Dong, M., Liu, D.R., Center for Structural Genomics of Infectious Diseases (CSGID)

Description: Crystals Structure of the Mutated Protease Domain of Botulinum Neurotoxin X (X4130B1).
[[Category: Unreleased Structures]]
[[Category: Dong, M]]
[[Category: Satchell, K.J.F]]
[[Category: Minasov, G]]
[[Category: Zhang, S]]
[[Category: Blum, T.R]]
[[Category: Liu, D.R]]
[[Category: Xiong, X]]
[[Category: Packer, M.S]]
[[Category: Liu, H]]
[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]
[[Category: Richter, M]]
[[Category: Lee, P.G]]