7xtn

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7xtn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XTN FirstGlance]. <br>
<table><tr><td colspan='2'>[[7xtn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombyx_mori Bombyx mori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XTN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=7xtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xtn OCA], [https://pdbe.org/7xtn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xtn RCSB], [https://www.ebi.ac.uk/pdbsum/7xtn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xtn 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=7xtn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xtn OCA], [https://pdbe.org/7xtn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xtn RCSB], [https://www.ebi.ac.uk/pdbsum/7xtn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xtn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/A0A6J2JXS5_BOMMA A0A6J2JXS5_BOMMA]]
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[https://www.uniprot.org/uniprot/A0A6J2JXS5_BOMMA A0A6J2JXS5_BOMMA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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N-glycans are modified by glycosyltransferases in the endoplasmic reticulum and Golgi apparatus. N-acetylglucosaminyltransferase IV (GnT-IV) is a Golgi-localized glycosyltransferase that synthesizes complex-type N-glycans in vertebrates. This enzyme attaches N-acetylglucosamine (GlcNAc) to the alpha-1,3-linked mannose branch of the N-glycan core structure via a beta-1,4 linkage. Deficiency of this enzyme is known to cause abnormal cellular functions, making it a vital enzyme for living organisms. However, there has been no report on its three-dimensional structure to date. Here, we demonstrated that the C-terminal regions (named CBML) of human GnT-IVa and Bombyx mori ortholog have the ability to bind beta-N-acetylglucosamine. Additionally, we determined the crystal structures of human CBML, B. mori CBML, and its complex with beta-GlcNAc at 1.97, 1.47, and 1.15 A resolutions, respectively, and showed that they adopt a beta-sandwich fold, similar to carbohydrate-binding module family 32 (CBM32) proteins. The regions homologous to CBML (&gt;/=24 percent identity) were found in GnT-IV isozymes, GnT-IVb, and GnT-IVc (known as GnT-VI), and the structure of B. mori CBML in complex with beta-GlcNAc indicated that the GlcNAc-binding residues were highly conserved among these isozymes. These residues are also conserved with the GlcNAc-binding CBM32 domain of beta-N-acetylhexosaminidase NagH from Clostridium perfringens despite the low sequence identity (&lt;20 percent). Taken together with the phylogenetic analysis, these findings indicate that these CBMLs may be novel CBM family proteins with GlcNAc-binding ability.
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Crystal structure and sugar-binding ability of the C-terminal domain of N-acetylglucosaminyltransferase IV establish a new carbohydrate-binding module family.,Oka N, Mori S, Ikegaya M, Park EY, Miyazaki T Glycobiology. 2022 Sep 15. pii: 6700080. doi: 10.1093/glycob/cwac058. PMID:36106687<ref>PMID:36106687</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7xtn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of the C-terminal domain of Bombyx mori N-acetylglucosaminyltransferase IV in complex with N-acetylglucosamine

PDB ID 7xtn

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