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3cv5

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Revision as of 13:39, 7 November 2018

GOLGI MANNOSIDASE II D204A catalytic nucleophile mutant complex with 3alpha,6alpha-mannopentaose

Structural highlights

3cv5 is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1hty, 1hww, 1hxk, 1ps2, 1qwn, 1qwu, 1qx1, 1r33, 1r34, 2alw, 2f7o, 2f7p, 2f7q, 2f7r, 3bub, 3bud, 3bui, 3bup, 3buq, 3bvt, 3bvu, 3bvv, 3bvw, 3bvx
Gene:	alpha-Man-II, GmII (Drosophila melanogaster)
Activity:	Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, with EC number 3.2.1.114
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shah N, Kuntz DA, Rose DR. Golgi alpha-mannosidase II cleaves two sugars sequentially in the same catalytic site. Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9570-5. Epub 2008 Jul 3. PMID:18599462

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3cv5"

@@ Line 1: / Line 1: @@
 ==GOLGI MANNOSIDASE II D204A catalytic nucleophile mutant complex with 3alpha,6alpha-mannopentaose==
 <StructureSection load='3cv5' size='340' side='right' caption='[[3cv5]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alpha-Man-II, GmII ([http://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'>[http://en.wikipedia.org/wiki/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cv5 OCA], [http://pdbe.org/3cv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cv5 RCSB], [http://www.ebi.ac.uk/pdbsum/3cv5 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cv5 OCA], [http://pdbe.org/3cv5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cv5 RCSB], [http://www.ebi.ac.uk/pdbsum/3cv5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3cv5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/3cv5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/3cv5_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3cv5

From Proteopedia

Revision as of 13:39, 7 November 2018

GOLGI MANNOSIDASE II D204A catalytic nucleophile mutant complex with 3alpha,6alpha-mannopentaose

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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