Proteopedia

3eju: Difference between revisions

← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='3eju' size='340' side='right'caption='[[3eju]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
<StructureSection load='3eju' size='340' side='right'caption='[[3eju]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3eju]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EJU FirstGlance]. <br>
<table><tr><td colspan='2'>[[3eju]] 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=3EJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EJU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HN7:1-(4-TERT-BUTYLPHENYL)-2-[(1S,2R,5S,8R,8AR)-1,2,8-TRIHYDROXYOCTAHYDROINDOLIZIN-5-YL]ETHANONE'>HN7</scene>, <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=ZN:ZINC+ION'>ZN</scene></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]] 1.32&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hty|1hty]], [[1hww|1hww]], [[1hxk|1hxk]], [[1ps2|1ps2]], [[1qwn|1qwn]], [[1r33|1r33]], [[1r34|1r34]], [[1tqv|1tqv]], [[2alw|2alw]], [[2f7o|2f7o]], [[2f7p|2f7p]], [[2f7q|2f7q]], [[2f7r|2f7r]], [[2fyv|2fyv]], [[3bub|3bub]], [[3bup|3bup]], [[3czn|3czn]], [[3ejp|3ejp]], [[3ejq|3ejq]], [[3ejr|3ejr]], [[3ejs|3ejs]], [[3ejt|3ejt]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HN7:1-(4-TERT-BUTYLPHENYL)-2-[(1S,2R,5S,8R,8AR)-1,2,8-TRIHYDROXYOCTAHYDROINDOLIZIN-5-YL]ETHANONE'>HN7</scene>, <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=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alpha-Man-II, GmII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] </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=3eju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eju OCA], [https://pdbe.org/3eju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eju RCSB], [https://www.ebi.ac.uk/pdbsum/3eju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eju ProSAT]</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=3eju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eju OCA], [https://pdbe.org/3eju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eju RCSB], [https://www.ebi.ac.uk/pdbsum/3eju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eju ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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).  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 22: Line 20:
</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=3eju 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=3eju ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Golgi alpha-mannosidase II (GMII) is a key enzyme in the N-glycosylation pathway and is a potential target for cancer chemotherapy. The natural product swainsonine is a potent inhibitor of GMII. In this paper we characterize the binding of 5alpha-substituted swainsonine analogues to the soluble catalytic domain of Drosophila GMII by X-ray crystallography. These inhibitors enjoy an advantage over previously reported GMII inhibitors in that they did not significantly decrease the inhibitory potential of the swainsonine head-group. The phenyl groups of these analogues occupy a portion of the binding site not previously seen to be populated with either substrate analogues or other inhibitors and they form novel hydrophobic interactions. They displace a well-organized water cluster, but the presence of a C(10) carbonyl allows the reestablishment of important hydrogen bonds. Already approximately tenfold more active against the Golgi enzyme than the lysosomal enzyme, these inhibitors offer the potential of being extended into the N-acetylglucosamine binding site of GMII for the creation of even more potent and selective GMII inhibitors.
Structural Investigation of the Binding of 5-Substituted Swainsonine Analogues to Golgi alpha-Mannosidase II.,Kuntz DA, Nakayama S, Shea K, Hori H, Uto Y, Nagasawa H, Rose DR Chembiochem. 2010 Mar 5;11(5):673-680. PMID:20209559<ref>PMID:20209559</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3eju" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drome]]
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]
[[Category: Kuntz DA]]
[[Category: Kuntz, D A]]
[[Category: Rose DR]]
[[Category: Rose, D R]]
[[Category: Shea K]]
[[Category: Shea, K]]
[[Category: Gh38 glycosidase]]
[[Category: Glycosidase]]
[[Category: Golgi apparatus]]
[[Category: Hydrolase]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Signal-anchor]]
[[Category: Transmembrane]]

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

OCA
Retrieved from "https://proteopedia.openfox.io/w/3eju"