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1hww
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1hww" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hww, resolution 1.87Å" /> '''GOLGI ALPHA-MANNOSID...) |
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| - | [[Image:1hww.gif|left|200px]]<br /><applet load="1hww" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1hww, resolution 1.87Å" /> | ||
| - | '''GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE'''<br /> | ||
| - | == | + | ==GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE== |
| - | Golgi alpha-mannosidase II, a key enzyme in N-glycan processing, is a | + | <StructureSection load='1hww' size='340' side='right'caption='[[1hww]], [[Resolution|resolution]] 1.87Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1hww]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HWW FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SWA:1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL'>SWA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1hww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hww OCA], [https://pdbe.org/1hww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hww RCSB], [https://www.ebi.ac.uk/pdbsum/1hww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hww ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MAN2_DROME MAN2_DROME] Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity). | ||
| + | == 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/hw/1hww_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=1hww ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Golgi alpha-mannosidase II, a key enzyme in N-glycan processing, is a target in the development of anti- cancer therapies. The crystal structure of Drosophila Golgi alpha-mannosidase II in the absence and presence of the anti-cancer agent swainsonine and the inhibitor deoxymannojirimycin reveals a novel protein fold with an active site zinc intricately involved both in the substrate specificity of the enzyme and directly in the catalytic mechanism. Identification of a putative GlcNAc binding pocket in the vicinity of the active site cavity provides a model for the binding of the GlcNAcMan(5)GlcNAc(2) substrate and the consecutive hydrolysis of the alpha1,6- and alpha1,3-linked mannose residues. The enzyme-inhibitor interactions observed provide insight into the catalytic mechanism, opening the door to the design of novel inhibitors of alpha-mannosidase II. | ||
| - | + | Structure of Golgi alpha-mannosidase II: a target for inhibition of growth and metastasis of cancer cells.,van den Elsen JM, Kuntz DA, Rose DR EMBO J. 2001 Jun 15;20(12):3008-17. PMID:11406577<ref>PMID:11406577</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1hww" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Mannosidase 3D structures|Mannosidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kuntz DA]] | ||
| + | [[Category: Rose DR]] | ||
| + | [[Category: Van den Elsen JMH]] | ||
Current revision
GOLGI ALPHA-MANNOSIDASE II IN COMPLEX WITH SWAINSONINE
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