4xso

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<StructureSection load='4xso' size='340' side='right'caption='[[4xso]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='4xso' size='340' side='right'caption='[[4xso]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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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]] 2.01&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xsp|4xsp]], [[4xsr|4xsr]], [[4xsu|4xsu]]</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=GOL:GLYCEROL'>GOL</scene></td></tr>
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<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>
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<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>
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<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>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8YQW3_NOSS1 Q8YQW3_NOSS1]
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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&amp;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.
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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<ref>PMID:26692049</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 4xso" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Anabaena 7120]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, Y X]]
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[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
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[[Category: Cheng, W]]
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[[Category: Chen YX]]
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[[Category: Dai, Y N]]
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[[Category: Cheng W]]
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[[Category: Jiang, Y L]]
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[[Category: Dai YN]]
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[[Category: Wang, X P]]
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[[Category: Jiang YL]]
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[[Category: Zhou, C Z]]
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[[Category: Wang XP]]
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[[Category: Glycosyltransferase]]
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[[Category: Zhou CZ]]
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[[Category: Gt-b fold]]
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[[Category: Transferase]]
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Current revision

Crystal structure of apo-form Alr3699/HepE from Anabaena sp. strain PCC 7120

PDB ID 4xso

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