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.


3sxg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:11, 14 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3sxg' size='340' side='right'caption='[[3sxg]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
<StructureSection load='3sxg' size='340' side='right'caption='[[3sxg]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3sxg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SXG FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3sxg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SXG FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 1.86&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sx3|3sx3]], [[3sx5|3sx5]], [[3sx7|3sx7]], [[3sx8|3sx8]], [[3sxa|3sxa]], [[3sxb|3sxb]], [[3sxc|3sxc]], [[3sxd|3sxd]], [[3sxe|3sxe]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABO ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glycoprotein-fucosylgalactoside_alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.40 2.4.1.40] </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=3sxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sxg OCA], [https://pdbe.org/3sxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sxg RCSB], [https://www.ebi.ac.uk/pdbsum/3sxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sxg 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=3sxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sxg OCA], [https://pdbe.org/3sxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sxg RCSB], [https://www.ebi.ac.uk/pdbsum/3sxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sxg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN]] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
+
[https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The human ABO(H) A and B blood group glycosyltransferases GTA and GTB differ by only four amino acids, yet this small dissimilarity is responsible for significant differences in biosynthesis, kinetics and structure. Like other glycosyltransferases, these two enzymes have been shown to recognize substrates through dramatic conformational changes in mobile polypeptide loops surrounding the active site. Structures of GTA, GTB and several chimeras determined by single-crystal X-ray diffraction demonstrate a range of susceptibility to the choice of cryoprotectant, in which the mobile polypeptide loops can be induced by glycerol to form the ordered closed conformation associated with substrate recognition and by MPD [hexylene glycol, (+/-)-2-methyl-2,4-pentanediol] to hinder binding of substrate in the active site owing to chelation of the Mn(2+) cofactor and thereby adopt the disordered open state. Glycerol is often avoided as a cryoprotectant when determining the structures of carbohydrate-active enzymes as it may act as a competitive inhibitor for monosaccharide ligands. Here, it is shown that the use of glycerol as a cryoprotectant can additionally induce significant changes in secondary structure, a phenomenon that could apply to any class of protein.
+
-
 
+
-
Sequence-dependent effects of cryoprotectants on the active sites of the human ABO(H) blood group A and B glycosyltransferases.,Johal AR, Schuman B, Alfaro JA, Borisova S, Seto NO, Evans SV Acta Crystallogr D Biol Crystallogr. 2012 Mar;68(Pt 3):268-76. Epub 2012 Feb 14. PMID:22349229<ref>PMID:22349229</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3sxg" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase]]
+
[[Category: Homo sapiens]]
-
[[Category: Human]]
+
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Evans, S V]]
+
[[Category: Evans SV]]
-
[[Category: Johal, A R]]
+
[[Category: Johal AR]]
-
[[Category: Abo rossmann fold]]
+
-
[[Category: Blood group antigen]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Manganese]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Retaining glycosyltransferase]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of AAAA+UDP+Gal with MPD as the cryoprotectant

PDB ID 3sxg

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/3sxg"
Personal tools