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| - | [[Image:1hn0.gif|left|200px]] | |
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| - | {{Structure
| + | ==CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION== |
| - | |PDB= 1hn0 |SIZE=350|CAPTION= <scene name='initialview01'>1hn0</scene>, resolution 1.90Å
| + | <StructureSection load='1hn0' size='340' side='right'caption='[[1hn0]], [[Resolution|resolution]] 1.90Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | <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> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Chondroitin-sulfate-ABC_endolyase Chondroitin-sulfate-ABC endolyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.20 4.2.2.20]
| + | </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> |
| - | |GENE=
| + | <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> |
| - | | + | </table> |
| - | '''CRYSTAL STRUCTURE OF CHONDROITIN ABC LYASE I FROM PROTEUS VULGARIS AT 1.9 ANGSTROMS RESOLUTION'''
| + | == 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> |
| - | | + | == Evolutionary Conservation == |
| - | ==Overview== | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | 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.
| + | Check<jmol> |
| - | | + | <jmolCheckbox> |
| - | ==About this Structure== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hn/1hn0_consurf.spt"</scriptWhenChecked> |
| - | 1HN0 is a [[Single protein]] 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].
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | | + | <text>to colour the structure by Evolutionary Conservation</text> |
| - | ==Reference== | + | </jmolCheckbox> |
| - | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12706721 12706721]
| + | </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]. |
| - | [[Category: Chondroitin-sulfate-ABC endolyase]] | + | <div style="clear:both"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Proteus vulgaris]] | | [[Category: Proteus vulgaris]] |
| - | [[Category: Single protein]]
| + | [[Category: Cygler M]] |
| - | [[Category: Cygler, M.]] | + | [[Category: Huang W]] |
| - | [[Category: Huang, W.]] | + | |
| - | [[Category: NA]]
| + | |
| - | [[Category: chondroitinase abc i]]
| + | |
| - | [[Category: chonroitin digestion]]
| + | |
| - | [[Category: mechanism]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:39:08 2008''
| + | |
| Structural highlights
Function
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).[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Prabhakar V, Capila I, Bosques CJ, Pojasek K, Sasisekharan R. Chondroitinase ABC I from Proteus vulgaris: cloning, recombinant expression and active site identification. Biochem J. 2005 Feb 15;386(Pt 1):103-12. PMID:15691229 doi:http://dx.doi.org/10.1042/BJ20041222
- ↑ Crespo D, Asher RA, Lin R, Rhodes KE, Fawcett JW. How does chondroitinase promote functional recovery in the damaged CNS? Exp Neurol. 2007 Aug;206(2):159-71. Epub 2007 May 8. PMID:17572406 doi:http://dx.doi.org/10.1016/j.expneurol.2007.05.001
- ↑ Hamai A, Hashimoto N, Mochizuki H, Kato F, Makiguchi Y, Horie K, Suzuki S. Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides. J Biol Chem. 1997 Apr 4;272(14):9123-30. PMID:9083041
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