1y6f

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[[Image:1y6f.gif|left|200px]]
 
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{{Structure
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==alpha-glucosyltransferase in complex with UDP-glucose and DNA containing an abasic site==
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|PDB= 1y6f |SIZE=350|CAPTION= <scene name='initialview01'>1y6f</scene>, resolution 2.4&Aring;
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<StructureSection load='1y6f' size='340' side='right'caption='[[1y6f]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=UPG:URIDINE-5&#39;-DIPHOSPHATE-GLUCOSE'>UPG</scene>, <scene name='pdbligand=UDP:URIDINE-5&#39;-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
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<table><tr><td colspan='2'>[[1y6f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y6F FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/DNA_alpha-glucosyltransferase DNA alpha-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.26 2.4.1.26]
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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]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></td></tr>
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}}
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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=1y6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y6f OCA], [https://pdbe.org/1y6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y6f RCSB], [https://www.ebi.ac.uk/pdbsum/1y6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y6f ProSAT]</span></td></tr>
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</table>
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'''alpha-glucosyltransferase in complex with UDP-glucose and DNA containing an abasic site'''
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== Function ==
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[https://www.uniprot.org/uniprot/GSTA_BPT4 GSTA_BPT4] Is involved in a DNA modification process to protect the phage genome against its own nucleases and the host restriction endonuclease system.
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__TOC__
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==Overview==
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</StructureSection>
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The Escherichia coli T4 bacteriophage uses two glycosyltransferases to glucosylate and thus protect its DNA: the retaining alpha-glucosyltransferase (AGT) and the inverting beta-glucosyltransferase (BGT). They glucosylate 5-hydroxymethyl cytosine (5-HMC) bases of duplex DNA using UDP-glucose as the sugar donor to form an alpha-glucosidic linkage and a beta-glucosidic linkage, respectively. Five structures of AGT have been determined: a binary complex with the UDP product and four ternary complexes with UDP or UDP-glucose and oligonucleotides containing an A:G, HMU:G (hydroxymethyl uracyl) or AP:G (apurinic/apyrimidinic) mismatch at the target base-pair. AGT adopts the GT-B fold, one of the two folds known for GTs. However, while the sugar donor binding mode is classical for a GT-B enzyme, the sugar acceptor binding mode is unexpected and breaks the established consensus: AGT is the first GT-B enzyme that predominantly binds both the sugar donor and acceptor to the C-terminal domain. Its active site pocket is highly similar to four retaining GT-B glycosyltransferases (trehalose-6-phosphate synthase, glycogen synthase, glycogen and maltodextrin phosphorylases) strongly suggesting a common evolutionary origin and catalytic mechanism for these enzymes. Structure-guided mutagenesis and kinetic analysis do not permit identification of a nucleophile residue responsible for a glycosyl-enzyme intermediate for the classical double displacement mechanism. Interestingly, the DNA structures reveal partially flipped-out bases. They provide evidence for a passive role of AGT in the base-flipping mechanism and for its specific recognition of the acceptor base.
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[[Category: Escherichia virus T4]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Lariviere L]]
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1Y6F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y6F OCA].
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[[Category: Morera S]]
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[[Category: Sommer N]]
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==Reference==
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Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase., Lariviere L, Sommer N, Morera S, J Mol Biol. 2005 Sep 9;352(1):139-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16081100 16081100]
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[[Category: Bacteriophage t4]]
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[[Category: DNA alpha-glucosyltransferase]]
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[[Category: Single protein]]
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[[Category: Lariviere, L.]]
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[[Category: Morera, S.]]
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[[Category: Sommer, N.]]
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[[Category: GOL]]
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[[Category: PEG]]
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[[Category: UDP]]
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[[Category: UPG]]
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[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:18:51 2008''
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Current revision

alpha-glucosyltransferase in complex with UDP-glucose and DNA containing an abasic site

PDB ID 1y6f

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