1sxq

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(New page: 200px<br /><applet load="1sxq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sxq, resolution 1.8&Aring;" /> '''BGT in complex with a...)
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[[Image:1sxq.gif|left|200px]]<br /><applet load="1sxq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sxq, resolution 1.8&Aring;" />
 
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'''BGT in complex with a 13mer DNA containing a central C:G base pair and UDP'''<br />
 
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==Overview==
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==BGT in complex with a 13mer DNA containing a central C:G base pair and UDP==
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Beta-glucosyltransferase (BGT) is a DNA-modifying enzyme and a, glycosyltransferase. This inverting enzyme transfers glucose from, UDP-glucose to the 5-hydroxymethyl cytosine bases of T4 phage DNA. From, previous structural analyses we showed that Asp-100 and Asn-70 were, respectively, the catalytic base and the key residue for specific DNA, recognition (Lariviere, L., Gueguen-Chaignon, V., and Morera, S. (2003) J., Mol. Biol. 330, 1077-1086). Here, we supply biochemical evidence, supporting their essential roles in catalysis. We have also shown, previously that BGT uses a base-flipping mechanism to access, 5-hydroxymethyl cytosine (Lariviere, L., and Morera, S. (2002) J. Mol., Biol. 324, 483-490). Whether it is an active or a passive process remains, unclear, as is the case for all DNA cleaving and modifying enzymes. Here, we report two crystal structures: (i) BGT in complex with a 13-mer DNA, containing an A:G mismatch and (ii) BGT in a ternary complex with UDP and, an oligonucleotide containing a single central G:C base pair. The binary, structure reveals a specific complex with the flipped-out, mismatched, adenine exposed to the active site. Unexpectedly, the other structure, shows the non-productive binding of an intermediate flipped-out base. Our, structural analysis provides clear evidence for a passive process.
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<StructureSection load='1sxq' size='340' side='right'caption='[[1sxq]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1sxq]] is a 6 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=1SXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SXQ FirstGlance]. <br>
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1SXQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with UDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA_beta-glucosyltransferase DNA beta-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.27 2.4.1.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SXQ OCA].
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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]] 1.8&#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=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
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==Reference==
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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=1sxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sxq OCA], [https://pdbe.org/1sxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sxq RCSB], [https://www.ebi.ac.uk/pdbsum/1sxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sxq ProSAT]</span></td></tr>
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Structural evidence of a passive base-flipping mechanism for beta-glucosyltransferase., Lariviere L, Morera S, J Biol Chem. 2004 Aug 13;279(33):34715-20. Epub 2004 Jun 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15178685 15178685]
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</table>
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[[Category: Bacteriophage t4]]
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== Function ==
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[[Category: DNA beta-glucosyltransferase]]
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[https://www.uniprot.org/uniprot/GSTB_BPT4 GSTB_BPT4] Catalyzes the transfer of glucose (Glc) from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA. 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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[[Category: Single protein]]
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__TOC__
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[[Category: Lariviere, L.]]
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</StructureSection>
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[[Category: Morera, S.]]
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[[Category: Escherichia virus T4]]
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[[Category: UDP]]
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[[Category: Large Structures]]
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[[Category: flipped-out base]]
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[[Category: Lariviere L]]
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[[Category: Morera S]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:49:32 2007''
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Current revision

BGT in complex with a 13mer DNA containing a central C:G base pair and UDP

PDB ID 1sxq

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