5gz8: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(One intermediate revision by the same user not shown)
Line 1: Line 1:


==Crystal structure of catalytic domain of Protein O-mannosyl Kinase in ligand-free form==
==Crystal structure of catalytic domain of Protein O-mannosyl Kinase in ligand-free form==
<StructureSection load='5gz8' size='340' side='right' caption='[[5gz8]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='5gz8' size='340' side='right'caption='[[5gz8]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5gz8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GZ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GZ8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5gz8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GZ8 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gz9|5gz9]]</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]] 2.5&#8491;</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=5gz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gz8 OCA], [http://pdbe.org/5gz8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gz8 RCSB], [http://www.ebi.ac.uk/pdbsum/5gz8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gz8 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=5gz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gz8 OCA], [https://pdbe.org/5gz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gz8 RCSB], [https://www.ebi.ac.uk/pdbsum/5gz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gz8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SG196_MOUSE SG196_MOUSE]] Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif (By similarity).  
[https://www.uniprot.org/uniprot/SG196_MOUSE SG196_MOUSE] Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 22: Line 22:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Nagae, M]]
[[Category: Large Structures]]
[[Category: Yamaguchi, Y]]
[[Category: Mus musculus]]
[[Category: Dystroglycanopathy]]
[[Category: Nagae M]]
[[Category: O-mannosylation]]
[[Category: Yamaguchi Y]]
[[Category: Sugar kinase]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/5gz8"