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| - | [[Image:1sxq.gif|left|200px]] | |
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| - | {{Structure
| + | ==BGT in complex with a 13mer DNA containing a central C:G base pair and UDP== |
| - | |PDB= 1sxq |SIZE=350|CAPTION= <scene name='initialview01'>1sxq</scene>, resolution 1.8Å
| + | <StructureSection load='1sxq' size='340' side='right'caption='[[1sxq]], [[Resolution|resolution]] 1.80Å' scene=''> |
| - | |SITE=
| + | == Structural highlights == |
| - | |LIGAND= <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene>
| + | <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> |
| - | |ACTIVITY= [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]
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | |GENE= BGT, BETA-GT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4])
| + | <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> |
| - | }}
| + | <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> |
| - | | + | </table> |
| - | '''BGT in complex with a 13mer DNA containing a central C:G base pair and UDP''' | + | == Function == |
| - | | + | [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. |
| - | | + | __TOC__ |
| - | ==Overview== | + | </StructureSection> |
| - | 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.
| + | [[Category: Escherichia virus T4]] |
| - | | + | [[Category: Large Structures]] |
| - | ==About this Structure== | + | [[Category: Lariviere L]] |
| - | 1SXQ 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=1SXQ OCA].
| + | [[Category: Morera S]] |
| - | | + | |
| - | ==Reference==
| + | |
| - | 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://www.ncbi.nlm.nih.gov/pubmed/15178685 15178685]
| + | |
| - | [[Category: Bacteriophage t4]] | + | |
| - | [[Category: DNA beta-glucosyltransferase]] | + | |
| - | [[Category: Single protein]] | + | |
| - | [[Category: Lariviere, L.]] | + | |
| - | [[Category: Morera, S.]] | + | |
| - | [[Category: UDP]]
| + | |
| - | [[Category: flipped-out base]]
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| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:11:00 2008''
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