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| | <StructureSection load='4xso' size='340' side='right'caption='[[4xso]], [[Resolution|resolution]] 2.01Å' scene=''> | | <StructureSection load='4xso' size='340' side='right'caption='[[4xso]], [[Resolution|resolution]] 2.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4xso]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XSO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4xso]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XSO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xsp|4xsp]], [[4xsr|4xsr]], [[4xsu|4xsu]]</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=4xso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xso OCA], [https://pdbe.org/4xso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xso RCSB], [https://www.ebi.ac.uk/pdbsum/4xso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xso ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr3699 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</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=4xso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xso OCA], [http://pdbe.org/4xso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xso RCSB], [http://www.ebi.ac.uk/pdbsum/4xso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xso ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8YQW3_NOSS1 Q8YQW3_NOSS1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Anabaena 7120]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, Y X]] | + | [[Category: Nostoc sp. PCC 7120 = FACHB-418]] |
| - | [[Category: Cheng, W]] | + | [[Category: Chen YX]] |
| - | [[Category: Dai, Y N]] | + | [[Category: Cheng W]] |
| - | [[Category: Jiang, Y L]] | + | [[Category: Dai YN]] |
| - | [[Category: Wang, X P]] | + | [[Category: Jiang YL]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Wang XP]] |
| - | [[Category: Glycosyltransferase]]
| + | [[Category: Zhou CZ]] |
| - | [[Category: Gt-b fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q8YQW3_NOSS1
Publication Abstract from PubMed
Formation of the heterocyst envelope polysaccharide (HEP) is a key process for cyanobacterial heterocyst differentiation. The maturation of HEP in Anabaena sp. strain PCC 7120 is controlled by a gene cluster termed HEP island in addition to an operon alr3698-alr3699, which encodes two putative proteins termed Alr3698/HepD and Alr3699/HepE. Here we report the crystal structures of HepE in the apo-form and three complex forms that bind to UDP-glucose (UDPG), UDP&glucose and UDP, respectively. The overall structure of HepE displays a typical GT-B fold of glycosyltransferases, comprising two separate beta/alpha/beta Rossmann-fold domains that form an inter-domain substrate-binding crevice. Structural analyses combined with enzymatic assays indicate that HepE is a glucosyltransferase using UDPG as a sugar donor. Further site-directed mutageneses enable us to assign the key residues that stabilize the sugar donor and putative acceptor. Based on the comparative structural analyses, we propose a putative catalytic cycle of HepE, which undergoes "open-closed-open" conformational changes upon binding to the substrates and release of products. These findings provide structural and catalytic insights into the first enzyme involved in the HEP biosynthesis pathway.
Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis.,Wang XP, Jiang YL, Dai YN, Cheng W, Chen Y, Zhou CZ Glycobiology. 2015 Dec 21. pii: cwv167. PMID:26692049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang XP, Jiang YL, Dai YN, Cheng W, Chen Y, Zhou CZ. Structural and enzymatic analyses of a glucosyltransferase Alr3699/HepE involved in Anabaena heterocyst envelop polysaccharide biosynthesis. Glycobiology. 2015 Dec 21. pii: cwv167. PMID:26692049 doi:http://dx.doi.org/10.1093/glycob/cwv167
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