1hn0 - Revision history

OCA at 07:28, 7 February 2024

OCA — Wed, 07 Feb 2024 07:28:40 GMT

←Older revision		Revision as of 07:28, 7 February 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9Å</td></tr>
-	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https://en.wikipedia.org/wiki/Lyase Lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21]~~ </~~span~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [https://pdbe.org/1hn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1hn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn0 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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [https://pdbe.org/1hn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1hn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CABC1_PROVU CABC1_PROVU]] Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).<ref>PMID:15691229</ref> <ref>PMID:17572406</ref> <ref>PMID:9083041</ref>	+	[https://www.uniprot.org/uniprot/CABC1_PROVU CABC1_PROVU] Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).<ref>PMID:15691229</ref> <ref>PMID:17572406</ref> <ref>PMID:9083041</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 20:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hn0 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hn0 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Chondroitin Sulfate ABC lyase I from Proteus vulgaris is an endolytic, broad-specificity glycosaminoglycan lyase, which degrades chondroitin, chondroitin-4-sulfate, dermatan sulfate, chondroitin-6-sulfate, and hyaluronan by beta-elimination of 1,4-hexosaminidic bond to unsaturated disaccharides and tetrasaccharides. Its structure revealed three domains. The N-terminal domain has a fold similar to that of carbohydrate-binding domains of xylanases and some lectins, the middle and C-terminal domains are similar to the structures of the two-domain chondroitin lyase AC and bacterial hyaluronidases. Although the middle domain shows a very low level of sequence identity with the catalytic domains of chondroitinase AC and hyaluronidase, the residues implicated in catalysis of the latter enzymes are present in chondroitinase ABC I. The substrate-binding site in chondroitinase ABC I is in a wide-open cleft, consistent with the endolytic action pattern of this enzyme. The tryptophan residues crucial for substrate binding in chondroitinase AC and hyaluronidases are lacking in chondroitinase ABC I. The structure of chondroitinase ABC I provides a framework for probing specific functions of active-site residues for understanding the remarkably broad specificity of this enzyme and perhaps engineering a desired specificity. The electron density map showed clearly that the deposited DNA sequence for residues 495-530 of chondroitin ABC lyase I, the segment containing two putative active-site residues, contains a frame-shift error resulting in an incorrectly translated amino acid sequence.
-
-	Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution.,Huang W, Lunin VV, Li Y, Suzuki S, Sugiura N, Miyazono H, Cygler M J Mol Biol. 2003 May 2;328(3):623-34. PMID:12706721<ref>PMID:12706721</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1hn0" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 34:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Lyase]]
	[[Category: Proteus vulgaris]]		[[Category: Proteus vulgaris]]
-	[[Category: Cygler, M]]	+	[[Category: Cygler M]]
-	[[Category: Huang, W]]	+	[[Category: Huang W]]
-	~~[[Category: Chondroitinase abc i]]~~	+
-	~~[[Category: Chonroitin digestion~~]]	+

OCA at 05:49, 28 April 2021

OCA — Wed, 28 Apr 2021 05:49:54 GMT

←Older revision		Revision as of 05:49, 28 April 2021
Line 3:		Line 3:
	<StructureSection load='1hn0' size='340' side='right'caption='[[1hn0]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1hn0' size='340' side='right'caption='[[1hn0]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Lyase Lyase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lyase Lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [~~http~~://pdbe.org/1hn0 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1hn0 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn0 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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [https://pdbe.org/1hn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1hn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CABC1_PROVU CABC1_PROVU]] Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).<ref>PMID:15691229</ref> <ref>PMID:17572406</ref> <ref>PMID:9083041</ref>	+	[[https://www.uniprot.org/uniprot/CABC1_PROVU CABC1_PROVU]] Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).<ref>PMID:15691229</ref> <ref>PMID:17572406</ref> <ref>PMID:9083041</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:32, 3 July 2019

OCA — Wed, 03 Jul 2019 07:32:19 GMT

←Older revision		Revision as of 07:32, 3 July 2019
Line 1:		Line 1:

	==CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION==		==CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION==
-	<StructureSection load='1hn0' size='340' side='right' caption='[[1hn0]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='1hn0' size='340' side='right'caption='[[1hn0]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>
Line 14:		Line 14:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hn0_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hn0_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 33:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Proteus vulgaris]]		[[Category: Proteus vulgaris]]

OCA at 10:55, 27 September 2017

OCA — Wed, 27 Sep 2017 10:55:08 GMT

←Older revision		Revision as of 10:55, 27 September 2017
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION==		==CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION==
	<StructureSection load='1hn0' size='340' side='right' caption='[[1hn0]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='1hn0' size='340' side='right' caption='[[1hn0]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://pdbe.org/1hn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://pdbe.org/1hn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hn0 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hn0 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 08:31, 11 September 2015

OCA — Fri, 11 Sep 2015 08:31:33 GMT

←Older revision		Revision as of 08:31, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://pdbe.org/1hn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/~~CABC_PROVU CABC_PROVU~~]] Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).<ref>PMID:~~9083041~~</ref> <ref>PMID:~~15691229~~</ref> <ref>PMID:~~17572406~~</ref>	+	[[http://www.uniprot.org/uniprot/CABC1_PROVU CABC1_PROVU]] Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).<ref>PMID:15691229</ref> <ref>PMID:17572406</ref> <ref>PMID:9083041</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 27:		Line 27:
	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 1hn0" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:54, 25 December 2014

OCA — Thu, 25 Dec 2014 13:54:30 GMT

←Older revision		Revision as of 13:54, 25 December 2014
Line 7:		Line 7:
	<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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CABC_PROVU CABC_PROVU]] Endolytic, broad-specificity glycosaminoglycan lyase, which degrades the polysaccharides chondroitin, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan sulfate and to a lesser extent hyaluronan, by beta-elimination of 1,4-hexosaminidic bond to unsaturated tetrasaccharides and disaccharides. Is not active against keratan sulfate, heparan sulfate, and heparin. Is able to promote functional recovery in the injured central nervous system (CNS), via its role in the disruption of the normal organization of the extracellular matrix (ECM).<ref>PMID:9083041</ref> <ref>PMID:15691229</ref> <ref>PMID:17572406</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 22:54, 22 December 2014

OCA — Mon, 22 Dec 2014 22:54:54 GMT

←Older revision		Revision as of 22:54, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 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=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 31:		Line 31:
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Proteus vulgaris]]		[[Category: Proteus vulgaris]]
-	[[Category: Cygler, M.]]	+	[[Category: Cygler, M]]
-	[[Category: Huang, W.]]	+	[[Category: Huang, W]]
	[[Category: Chondroitinase abc i]]		[[Category: Chondroitinase abc i]]
	[[Category: Chonroitin digestion]]		[[Category: Chonroitin digestion]]
-	[[Category: Lyase]]

OCA at 12:40, 28 September 2014

OCA — Sun, 28 Sep 2014 12:40:34 GMT

←Older revision		Revision as of 12:40, 28 September 2014
Line 1:		Line 1:
-	[[~~Image~~:1hn0.~~png\|left~~\|200px]]	+	==CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION==
		+	<StructureSection load='1hn0' size='340' side='right' caption='[[1hn0]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1hn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HN0 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 and 4.2.2.21 4.2.2.20 and 4.2.2.21] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hn0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hn0 RCSB], [http://www.ebi.ac.uk/pdbsum/1hn0 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hn0_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Chondroitin Sulfate ABC lyase I from Proteus vulgaris is an endolytic, broad-specificity glycosaminoglycan lyase, which degrades chondroitin, chondroitin-4-sulfate, dermatan sulfate, chondroitin-6-sulfate, and hyaluronan by beta-elimination of 1,4-hexosaminidic bond to unsaturated disaccharides and tetrasaccharides. Its structure revealed three domains. The N-terminal domain has a fold similar to that of carbohydrate-binding domains of xylanases and some lectins, the middle and C-terminal domains are similar to the structures of the two-domain chondroitin lyase AC and bacterial hyaluronidases. Although the middle domain shows a very low level of sequence identity with the catalytic domains of chondroitinase AC and hyaluronidase, the residues implicated in catalysis of the latter enzymes are present in chondroitinase ABC I. The substrate-binding site in chondroitinase ABC I is in a wide-open cleft, consistent with the endolytic action pattern of this enzyme. The tryptophan residues crucial for substrate binding in chondroitinase AC and hyaluronidases are lacking in chondroitinase ABC I. The structure of chondroitinase ABC I provides a framework for probing specific functions of active-site residues for understanding the remarkably broad specificity of this enzyme and perhaps engineering a desired specificity. The electron density map showed clearly that the deposited DNA sequence for residues 495-530 of chondroitin ABC lyase I, the segment containing two putative active-site residues, contains a frame-shift error resulting in an incorrectly translated amino acid sequence.

-	~~{{STRUCTURE_1hn0\| PDB=1hn0 \| SCENE= }}~~	+	Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution.,Huang W, Lunin VV, Li Y, Suzuki S, Sugiura N, Miyazono H, Cygler M J Mol Biol. 2003 May 2;328(3):623-34. PMID:12706721<ref>PMID:12706721</ref>

-	~~===CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_12706721}}~~	+	== References ==
-		+	<references/>
-	~~==About this Structure==~~	+	__TOC__
-	~~[[1hn0]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Proteus_vulgaris Proteus vulgaris]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA].~~	+	</StructureSection>
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:012706721<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Proteus vulgaris]]		[[Category: Proteus vulgaris]]

OCA: Protected "1hn0" [edit=sysop:move=sysop]

OCA — Wed, 21 Nov 2012 15:55:30 GMT

Protected "1hn0" [edit=sysop:move=sysop]

←Older revision

Revision as of 15:55, 21 November 2012

OCA at 15:55, 21 November 2012

OCA — Wed, 21 Nov 2012 15:55:28 GMT

←Older revision		Revision as of 15:55, 21 November 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1hn0.png\|left\|200px]]		[[Image:1hn0.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1hn0", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
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	{{STRUCTURE_1hn0\| PDB=1hn0 \| SCENE= }}		{{STRUCTURE_1hn0\| PDB=1hn0 \| SCENE= }}

	===CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION===		===CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_12706721}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 12706721 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_12706721}}		{{ABSTRACT_PUBMED_12706721}}

	==About this Structure==		==About this Structure==
-	~~1HN0~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA].	+	[[1hn0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proteus_vulgaris Proteus vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HN0 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~12706721~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:012706721</ref><references group="xtra"/>
-	[[Category: ~~Chondroitin-sulfate-ABC endolyase~~]]	+	[[Category: Lyase]]
	[[Category: Proteus vulgaris]]		[[Category: Proteus vulgaris]]
	[[Category: Cygler, M.]]		[[Category: Cygler, M.]]
Line 30:		Line 18:
	[[Category: Chondroitinase abc i]]		[[Category: Chondroitinase abc i]]
	[[Category: Chonroitin digestion]]		[[Category: Chonroitin digestion]]
-	[[Category: ~~Mechanism~~]]	+	[[Category: Lyase]]
-		+
-	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 17:58:40 2009''~~	+