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1hmu

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(New page: 200px<br /><applet load="1hmu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hmu, resolution 2.0&Aring;" /> '''ACTIVE SITE OF CHONDR...)
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[[Image:1hmu.gif|left|200px]]<br /><applet load="1hmu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hmu, resolution 2.0&Aring;" />
 
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'''ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS'''<br />
 
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==Overview==
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==ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS==
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The crystal structures of Flavobacterium heparinium chondroitin AC lyase, (chondroitinase AC; EC 4.2.2.5) bound to dermatan sulfate hexasaccharide, (DS(hexa)), tetrasaccharide (DS(tetra)), and hyaluronic acid, tetrasaccharide (HA(tetra)) have been refined at 2.0, 2.0, and 2.1 A, resolution, respectively. The structure of the Tyr234Phe mutant of AC, lyase bound to a chondroitin sulfate tetrasaccharide (CS(tetra)) has also, been determined to 2.3 A resolution. For each of these complexes, four, (DS(hexa) and CS(tetra)) or two (DS(tetra) and HA(tetra)) ordered sugars, are visible in electron density maps. The lyase AC DS(hexa) and CS(tetra), complexes reveal binding at four subsites, -2, -1, +1, and +2, within a, narrow and shallow protein channel. We suggest that subsites -2 and -1, together represent the substrate recognition area, +1 is the catalytic, subsite and +1 and +2 together represent the product release area. The, putative catalytic site is located between the substrate recognition area, and the product release area, carrying out catalysis at the +1 subsite., Four residues near the catalytic site, His225, Tyr234, Arg288, and Glu371, together form a catalytic tetrad. The mutations His225Ala, Tyr234Phe, Arg288Ala, and Arg292Ala, revealed residual activity for only the, Arg292Ala mutant. Structural data indicate that Arg292 is primarily, involved in recognition of the N-acetyl and sulfate moieties of, galactosamine, but does not participate directly in catalysis. Candidates, for the general base, removing the proton attached to C-5 of the, glucuronic acid at the +1 subsite, are Tyr234, which could be transiently, deprotonated during catalysis, or His225. Tyrosine 234 is a candidate to, protonate the leaving group. Arginine 288 likely contributes to charge, neutralization and stabilization of the enolate anion intermediate during, catalysis.
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<StructureSection load='1hmu' size='340' side='right'caption='[[1hmu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hmu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pedobacter_heparinus Pedobacter heparinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HMU FirstGlance]. <br>
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1HMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pedobacter_heparinus Pedobacter heparinus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Chondroitin_AC_lyase Chondroitin AC lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.5 4.2.2.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HMU OCA].
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASG:2-DEOXY-2-ACETAMIDO-BETA-D-GALACTOSE-4-SULFATE'>ASG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GCD:4,5-DEHYDRO-D-GLUCURONIC+ACID'>GCD</scene>, <scene name='pdbligand=GCU:D-GLUCURONIC+ACID'>GCU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MXY:2-O-METHYL+FUCOSE'>MXY</scene>, <scene name='pdbligand=RAM:ALPHA-L-RHAMNOSE'>RAM</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hmu OCA], [https://pdbe.org/1hmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hmu RCSB], [https://www.ebi.ac.uk/pdbsum/1hmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hmu ProSAT]</span></td></tr>
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Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis., Huang W, Boju L, Tkalec L, Su H, Yang HO, Gunay NS, Linhardt RJ, Kim YS, Matte A, Cygler M, Biochemistry. 2001 Feb 27;40(8):2359-72. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11327856 11327856]
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</table>
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[[Category: Chondroitin AC lyase]]
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== Function ==
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[https://www.uniprot.org/uniprot/CSLA_PEDHD CSLA_PEDHD]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/1hmu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1hmu ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pedobacter heparinus]]
[[Category: Pedobacter heparinus]]
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[[Category: Single protein]]
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[[Category: Boju L]]
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[[Category: Boju, L.]]
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[[Category: Cygler M]]
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[[Category: Cygler, M.]]
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[[Category: Gunay NS]]
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[[Category: Gunay, N.S.]]
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[[Category: Huang W]]
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[[Category: Huang, W.]]
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[[Category: Kim YS]]
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[[Category: Kim, Y.S.]]
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[[Category: Linhardt RJ]]
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[[Category: Linhardt, R.J.]]
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[[Category: Matte A]]
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[[Category: Matte, A.]]
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[[Category: Su H]]
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[[Category: Su, H.]]
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[[Category: Tkalec L]]
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[[Category: Tkalec, L.]]
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[[Category: Yang HO]]
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[[Category: Yang, H.O.]]
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[[Category: CA]]
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[[Category: active site]]
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[[Category: catalysis]]
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[[Category: protein-oligosaccharide complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:39:36 2007''
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Current revision

ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

PDB ID 1hmu

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