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.


4tqk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:00, 20 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Structural basis of specific recognition of non-reducing terminal N-acetylglucosamine by an Agrocybe aegerita lection==
==Structural basis of specific recognition of non-reducing terminal N-acetylglucosamine by an Agrocybe aegerita lection==
-
<StructureSection load='4tqk' size='340' side='right' caption='[[4tqk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+
<StructureSection load='4tqk' size='340' side='right'caption='[[4tqk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4tqk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TQK FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4tqk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyclocybe_aegerita Cyclocybe aegerita]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TQK FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.1&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tqj|4tqj]], [[4tqm|4tqm]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4tqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tqk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tqk RCSB], [http://www.ebi.ac.uk/pdbsum/4tqk PDBsum]</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=4tqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tqk OCA], [https://pdbe.org/4tqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tqk RCSB], [https://www.ebi.ac.uk/pdbsum/4tqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tqk ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/H6CS64_CYCAE H6CS64_CYCAE]
-
O-linked N-acetylglucosaminylation (O-GlcNAcylation) is a reversible post-translational modification that plays essential roles in many cellular pathways. Research in this field, however, is hampered by the lack of suitable probes to identify, accumulate, and purify the O-GlcNAcylated proteins. We have previously reported the identification of a lectin from the mushroom Agrocybe aegerita, i.e., Agrocybe aegerita lectin 2, or AAL2, that could bind terminal N-acetylglucosamine with higher affinities and specificity than other currently used probes. In this paper, we report the crystal structures of AAL2 and its complexes with GlcNAc and GlcNAcbeta1-3Galbeta1-4GlcNAc and reveal the structural basis of GlcNAc recognition by AAL2 and residues essential for the binding of terminal N-acetylglucosamine. Study on AAL2 may enable us to design a protein probe that can be used to identify and purify O-GlcNAcylated proteins more efficiently.
+
-
 
+
-
Structural Basis of Specific Recognition of Non-Reducing Terminal N-Acetylglucosamine by an Agrocybe aegerita Lectin.,Ren XM, Li DF, Jiang S, Lan XQ, Hu Y, Sun H, Wang DC PLoS One. 2015 Jun 26;10(6):e0129608. doi: 10.1371/journal.pone.0129608., eCollection 2015. PMID:26114302<ref>PMID:26114302</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Hu, Y L]]
+
[[Category: Cyclocybe aegerita]]
-
[[Category: Jiang, S]]
+
[[Category: Large Structures]]
-
[[Category: Lan, X Q]]
+
[[Category: Hu YL]]
-
[[Category: Li, D F]]
+
[[Category: Jiang S]]
-
[[Category: Ren, X M]]
+
[[Category: Lan XQ]]
-
[[Category: Sun, H]]
+
[[Category: Li DF]]
-
[[Category: Wang, D C]]
+
[[Category: Ren XM]]
-
[[Category: Complex]]
+
[[Category: Sun H]]
-
[[Category: Glcnac]]
+
[[Category: Wang DC]]
-
[[Category: Lectin]]
+
-
[[Category: Sugar binding protein]]
+

Current revision

Structural basis of specific recognition of non-reducing terminal N-acetylglucosamine by an Agrocybe aegerita lection

PDB ID 4tqk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools