1c90

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(New page: 200px<br /><applet load="1c90" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c90, resolution 2.1&Aring;" /> '''ENDO-BETA-N-ACETYLGLU...)
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[[Image:1c90.gif|left|200px]]<br /><applet load="1c90" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1c90, resolution 2.1&Aring;" />
 
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'''ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H, E132Q MUTANT'''<br />
 
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==Overview==
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==Endo-Beta-N-Acetylglucosaminidase H, E132Q Mutant==
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Endo-beta-N-acetylglucosaminidase H hydrolyzes the beta-(1-4)-glycosidic, link of the N,N'-diacetylchitobiose core of high-mannose and hybrid, asparagine-linked oligosaccharides. Seven mutants of the active site, residues, Asp130 and Glu132, have been prepared, assayed, and, crystallized. They include single site mutants of each residue to the, corresponding amide, to Ala and to the alternate acidic residue, and to, the double amide mutant. The mutants of Asp130 are more active than the, corresponding Glu132 mutants, consistent with the assignment of the latter, residue as the primary catalytic residue. The amide mutants are more, active than the alternate acidic residue mutants, which in turn are more, active than the Ala mutants. The structures of the Asn mutant of Asp130, and the double mutant are very similar to that of the wild-type enzyme., Several residues surrounding the mutated residues, including some that, form part of the core of the beta-barrel and especially Tyr168 and Tyr244, adopt a very different conformation in the structures of the other two, mutants of Asp130 and in the Asp mutant of Glu132. The results show that, the residues in the upper layers of the beta-barrel can organize into two, very distinct packing arrangements that depend on subtle electrostatic and, steric differences and that greatly affect the geometry of the, substrate-binding cleft. Consequently, the relative activities of several, of the mutants are defined by structural changes, leading to impaired, substrate binding, in addition to changes in functionality.
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<StructureSection load='1c90' size='340' side='right'caption='[[1c90]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1c90]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_plicatus Streptomyces plicatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C90 FirstGlance]. <br>
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1C90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_plicatus Streptomyces plicatus]. Active as [http://en.wikipedia.org/wiki/Mannosyl-glycoprotein_endo-beta-N-acetylglucosaminidase Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.96 3.2.1.96] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C90 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]] 2.1&#8491;</td></tr>
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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=1c90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c90 OCA], [https://pdbe.org/1c90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c90 RCSB], [https://www.ebi.ac.uk/pdbsum/1c90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c90 ProSAT]</span></td></tr>
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==Reference==
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</table>
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Mutations of endo-beta-N-acetylglucosaminidase H active site residueAs sp130 anG glu132: activities and conformations., Rao V, Cui T, Guan C, Van Roey P, Protein Sci. 1999 Nov;8(11):2338-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10595536 10595536]
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== Function ==
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[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
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[https://www.uniprot.org/uniprot/EBAG_STRPL EBAG_STRPL] Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.
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[[Category: Single protein]]
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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/c9/1c90_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=1c90 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: Streptomyces plicatus]]
[[Category: Streptomyces plicatus]]
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[[Category: Guan, C.]]
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[[Category: Guan C]]
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[[Category: Rao, V.]]
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[[Category: Rao V]]
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[[Category: Roey, P.Van.]]
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[[Category: Tao C]]
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[[Category: Tao, C.]]
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[[Category: Van Roey P]]
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[[Category: (beta/alpha)8 barrel]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:16:17 2007''
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Current revision

Endo-Beta-N-Acetylglucosaminidase H, E132Q Mutant

PDB ID 1c90

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