|
|
| (16 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
| [[Image:1edt.jpg|left|200px]]<br /><applet load="1edt" size="450" color="white" frame="true" align="right" spinBox="true"
| |
| caption="1edt, resolution 1.90Å" />
| |
| '''CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION'''<br />
| |
|
| |
|
| ==Overview== | | ==CRYSTAL STRUCTURE OF ENDO-BETA-N-ACETYLGLUCOSAMINIDASE H AT 1.9 ANGSTROMS RESOLUTION: ACTIVE SITE GEOMETRY AND SUBSTRATE RECOGNITION== |
| 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.
| | <StructureSection load='1edt' size='340' side='right'caption='[[1edt]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | | == Structural highlights == |
| ==About this Structure== | | <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> |
| 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].
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=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> |
| ==Reference== | | </table> |
| 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]
| | == Function == |
| [[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
| | [https://www.uniprot.org/uniprot/EBAG_STRPL EBAG_STRPL] Cleaves asparagine-linked oligomannose and hybrid, but not complex, oligosaccharides from glycoproteins. |
| [[Category: Single protein]] | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ed/1edt_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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]. |
| | <div style="clear:both"></div> |
| | __TOC__ |
| | </StructureSection> |
| | [[Category: Large Structures]] |
| [[Category: Streptomyces plicatus]] | | [[Category: Streptomyces plicatus]] |
| [[Category: Rao, V.]] | | [[Category: Rao V]] |
| [[Category: Roey, P.Van.]] | | [[Category: Van Roey P]] |
| [[Category: hydrolase (glucosidase)]]
| |
| | |
| ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:55:35 2007''
| |
