1edt

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(New page: 200px<br /><applet load="1edt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1edt, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1edt.jpg|left|200px]]<br /><applet load="1edt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1edt, resolution 1.90&Aring;" />
 
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'''CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION==
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BACKGROUND: Endo-beta-N-acetylglucosaminidase H (Endo H), an, endoglycosidase secreted by Streptomyces plicatus, hydrolyzes the, glycosidic bond between the core N-acetyglucosamine residues of, asparagine-linked high-mannose oligosaccharides. Endo H is a commonly used, reagent in glycobiology research, including the characterization of, oligosaccharides in glycoproteins. On-going crystallographic studies of, Endo H and related endoglycosidases are aimed at identifying the molecular, features that determine the different substrate specificities of these, enzymes. RESULTS: The three-dimensional structure of Endo H has been, determined to 1.9 A resolution. The overall fold of the enzyme is that of, an irregular (alpha/beta)8-barrel comprising eight, beta-strand/loop/alpha-helix units. Units 5 and 6 have very short loop, sections at the top of the molecule and their alpha-helices are replaced, by sections of extended geometry. The loop of unit 2 includes a small, two-stranded antiparallel beta-sheet. A shallow curved cleft runs across, the surface of the molecule from the area of units 5 and 6, over the core, of the beta-barrel to the area of the beta-sheet of loop 2. This cleft, contains the putative catalytic residues Asp130 and Glu132 above the core, of the beta-barrel. These residues are surrounded by several aromatic, residues. The loop 2 area of the cleft is formed by neutral polar, residues, mostly asparagines. CONCLUSIONS: The structure of Endo H is very, similar to that of Endo F1, a closely related endoglycosidase secreted by, Flavobacterium meningosepticum. Detailed comparison of the structures of, Endo H and Endo F1 supports the model previously proposed for substate, binding and recognition, in which the area of loop 2 determines the, substrate specificity and the alpha-helices of units 5 and 6 are missing, to accommodate the protein moiety of the substrate.
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<StructureSection load='1edt' size='340' side='right'caption='[[1edt]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1edt]] 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=1EDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EDT FirstGlance]. <br>
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1EDT 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=1EDT 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]] 1.9&#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=1edt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1edt OCA], [https://pdbe.org/1edt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1edt RCSB], [https://www.ebi.ac.uk/pdbsum/1edt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1edt ProSAT]</span></td></tr>
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==Reference==
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</table>
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Crystal structure of endo-beta-N-acetylglucosaminidase H at 1.9 A resolution: active-site geometry and substrate recognition., Rao V, Guan C, Van Roey P, Structure. 1995 May 15;3(5):449-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7663942 7663942]
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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/ed/1edt_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=1edt 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: Rao, V.]]
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[[Category: Rao V]]
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[[Category: Roey, P.Van.]]
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[[Category: Van Roey P]]
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[[Category: hydrolase (glucosidase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:55:35 2007''
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Current revision

CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION

PDB ID 1edt

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