1c92: Difference between revisions

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==Endo-Beta-N-Acetylglucosaminidase H, E132A Mutant==
==Endo-Beta-N-Acetylglucosaminidase H, E132A Mutant==
<StructureSection load='1c92' size='340' side='right' caption='[[1c92]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1c92' size='340' side='right'caption='[[1c92]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1c92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25483 Atcc 25483]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C92 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1c92]] is a 1 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=1C92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C92 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1edt|1edt]], [[1c8x|1c8x]], [[1c8y|1c8y]], [[1c90|1c90]], [[1c3f|1c3f]], [[1c91|1c91]], [[1c93|1c93]]</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]] 2.1&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=1c92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c92 OCA], [https://pdbe.org/1c92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c92 RCSB], [https://www.ebi.ac.uk/pdbsum/1c92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c92 ProSAT]</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=1c92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c92 OCA], [http://pdbe.org/1c92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1c92 RCSB], [http://www.ebi.ac.uk/pdbsum/1c92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1c92 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/EBAG_STRPL EBAG_STRPL]] Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.  
[https://www.uniprot.org/uniprot/EBAG_STRPL EBAG_STRPL] Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c92_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c92_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 20: Line 19:
</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=1c92 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=1c92 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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:10595536<ref>PMID:10595536</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1c92" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 25483]]
[[Category: Large Structures]]
[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
[[Category: Streptomyces plicatus]]
[[Category: Cui, T]]
[[Category: Cui T]]
[[Category: Guan, C]]
[[Category: Guan C]]
[[Category: Rao, V]]
[[Category: Rao V]]
[[Category: Roey, P Van]]
[[Category: Van Roey P]]
[[Category: Hydrolase]]

Latest revision as of 09:41, 7 February 2024

Endo-Beta-N-Acetylglucosaminidase H, E132A MutantEndo-Beta-N-Acetylglucosaminidase H, E132A Mutant

Structural highlights

1c92 is a 1 chain structure with sequence from Streptomyces plicatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EBAG_STRPL Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1c92, resolution 2.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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