This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3czs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:17, 20 October 2021) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3czs.png|left|200px]]
 
-
<!--
+
==Golgi alpha-mannosidase II (D204A nucleophile mutant)==
-
The line below this paragraph, containing "STRUCTURE_3czs", creates the "Structure Box" on the page.
+
<StructureSection load='3czs' size='340' side='right'caption='[[3czs]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[3czs]] 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=3CZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CZS FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]], [[1qwu|1qwu]], [[1qx1|1qx1]], [[1r33|1r33]], [[1r34|1r34]], [[2alw|2alw]], [[2f7o|2f7o]], [[2f7p|2f7p]], [[2f7q|2f7q]], [[2f7r|2f7r]], [[3bub|3bub]], [[3bud|3bud]], [[3bui|3bui]], [[3bup|3bup]], [[3buq|3buq]], [[3bvt|3bvt]], [[3bvu|3bvu]], [[3bvv|3bvv]], [[3bvw|3bvw]], [[3bvx|3bvx]], [[3cv5|3cv5]], [[3czn|3czn]], [[3d4y|3d4y]], [[3d4z|3d4z]], [[3d50|3d50]], [[3d51|3d51]], [[3d52|3d52]]</div></td></tr>
-
{{STRUCTURE_3czs| PDB=3czs | SCENE= }}
+
<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 Drosophila melanogaster])</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=3czs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3czs OCA], [https://pdbe.org/3czs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3czs RCSB], [https://www.ebi.ac.uk/pdbsum/3czs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3czs 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/cz/3czs_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=3czs ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Golgi alpha-mannosidase II (GMII) is a key glycosyl hydrolase in the N-linked glycosylation pathway. It catalyzes the removal of two different mannosyl linkages of GlcNAcMan(5)GlcNAc(2), which is the committed step in complex N-glycan synthesis. Inhibition of this enzyme has shown promise in certain cancers in both laboratory and clinical settings. Here we present the high-resolution crystal structure of a nucleophile mutant of Drosophila melanogaster GMII (dGMII) bound to its natural oligosaccharide substrate and an oligosaccharide precursor as well as the structure of the unliganded mutant. These structures allow us to identify three sugar-binding subsites within the larger active site cleft. Our results allow for the formulation of the complete catalytic process of dGMII, which involves a specific order of bond cleavage, and a major substrate rearrangement in the active site. This process is likely conserved for all GMII enzymes-but not in the structurally related lysosomal mannosidase-and will form the basis for the design of specific inhibitors against GMII.
-
===Golgi alpha-mannosidase II (D204A nucleophile mutant)===
+
Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site.,Shah N, Kuntz DA, Rose DR Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9570-5. Epub 2008 Jul 3. PMID:18599462<ref>PMID:18599462</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3czs" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_18599462}}, adds the Publication Abstract to the page
+
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 18599462 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_18599462}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
3CZS is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CZS OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:18599462</ref><references group="xtra"/>
+
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
 +
[[Category: Large Structures]]
[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]
[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]
-
[[Category: Rose, D R.]]
+
[[Category: Rose, D R]]
-
[[Category: Shah, N.]]
+
[[Category: Shah, N]]
-
[[Category: 2 c-terminal beta barrel]]
+
[[Category: C-terminal beta barrel]]
[[Category: Glycosyl hydrolase]]
[[Category: Glycosyl hydrolase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
Line 34: Line 49:
[[Category: N-terminal alpha-beta domain]]
[[Category: N-terminal alpha-beta domain]]
[[Category: Three helix bundle]]
[[Category: Three helix bundle]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 07:07:18 2009''
 

Current revision

Golgi alpha-mannosidase II (D204A nucleophile mutant)

PDB ID 3czs

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3czs"
Personal tools