1h4h

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{{Seed}}
 
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[[Image:1h4h.png|left|200px]]
 
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==Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre==
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The line below this paragraph, containing "STRUCTURE_1h4h", creates the "Structure Box" on the page.
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<StructureSection load='1h4h' size='340' side='right'caption='[[1h4h]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1h4h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salipaludibacillus_agaradhaerens Salipaludibacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H4H FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.9&#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=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene>, <scene name='pdbligand=XYS:XYLOPYRANOSE'>XYS</scene></td></tr>
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{{STRUCTURE_1h4h| PDB=1h4h | SCENE= }}
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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=1h4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4h OCA], [https://pdbe.org/1h4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h4h RCSB], [https://www.ebi.ac.uk/pdbsum/1h4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h4h ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7SIE2_SALAG Q7SIE2_SALAG]
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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/h4/1h4h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1h4h ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: The enzymatic hydrolysis of glycosides involves the formation and subsequent breakdown of a covalent glycosyl-enzyme intermediate via oxocarbenium-ion-like transition states. The covalent intermediate may be trapped on-enzyme using 2-fluoro-substituted glycosides, which provide details of the intermediate conformation and noncovalent interactions between enzyme and oligosaccharide. Xylanases are important in industrial applications - in the pulp and paper industry, pretreating wood with xylanases decreases the amount of chlorine-containing chemicals used. Xylanases are structurally similar to cellulases but differ in their specificity for xylose-based, versus glucose-based, substrates. RESULTS: The structure of the family 11 xylanase, Xyl11, from Bacillus agaradhaerens has been solved using X-ray crystallography in both native and xylobiosyl-enzyme intermediate forms at 1.78 A and 2.0 A resolution, respectively. The covalent glycosyl-enzyme intermediate has been trapped using a 2-fluoro-2-deoxy substrate with a good leaving group. Unlike covalent intermediate structures for glycoside hydrolases from other families, the covalent glycosyl-enzyme intermediate in family 11 adopts an unusual 2,5B conformation. CONCLUSIONS: The 2,5B conformation found for the alpha-linked xylobiosyl-enzyme intermediate of Xyl11, unlike the 4C1 chair conformation observed for other systems, is consistent with the stereochemical constraints required of the oxocarbenium-ion-like transition state. Comparison of the Xyl11 covalent glycosyl-enzyme intermediate with the equivalent structure for the related family 12 endoglucanase, CelB, from Streptomyces lividans reveals the likely determinants for substrate specificity in this clan of glycoside hydrolases.
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===OLIGOSACCHARIDE-BINDING TO FAMILY 11 XYLANASES: BOTH COVALENT INTERMEDIATE AND MUTANT-PRODUCT COMPLEXES DISPLAY 2,5B CONFORMATIONS AT THE ACTIVE-CENTRE===
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Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase.,Sabini E, Sulzenbacher G, Dauter M, Dauter Z, Jorgensen PL, Schulein M, Dupont C, Davies GJ, Wilson KS Chem Biol. 1999 Jul;6(7):483-92. PMID:10381409<ref>PMID:10381409</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11526340}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1h4h" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11526340 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11526340}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1H4H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H4H OCA].
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[[Category: Salipaludibacillus agaradhaerens]]
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[[Category: Danielsen S]]
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==Reference==
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[[Category: Davies GJ]]
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Oligosaccharide binding to family 11 xylanases: both covalent intermediate and mutant product complexes display (2,5)B conformations at the active centre., Sabini E, Wilson KS, Danielsen S, Schulein M, Davies GJ, Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1344-7. Epub 2001, Aug 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11526340 11526340]
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[[Category: Sabini E]]
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[[Category: Bacillus agaradhaerens]]
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[[Category: Schulein M]]
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Wilson KS]]
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[[Category: Single protein]]
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[[Category: Danielsen, S.]]
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[[Category: Davies, G J.]]
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[[Category: Sabini, E.]]
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[[Category: Schulein, M.]]
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[[Category: Wilson, K S.]]
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[[Category: Boat conformation]]
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[[Category: Intermediate]]
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[[Category: Mutant]]
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[[Category: Oligosaccharide]]
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[[Category: Transition-state]]
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[[Category: Xylanase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:36:30 2008''
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Current revision

Oligosaccharide-binding to family 11 xylanases: both covalent intermediate and mutant-product complexes display 2,5B conformations at the active-centre

PDB ID 1h4h

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