1ixy: Difference between revisions

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[[Image:1ixy.gif|left|200px]]


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==Ternary complex of T4 phage BGT with UDP and a 13 mer DNA duplex==
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<StructureSection load='1ixy' size='340' side='right'caption='[[1ixy]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ixy]] 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=1IXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IXY FirstGlance]. <br>
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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]] 2.5&#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=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
{{STRUCTURE_1ixy|  PDB=1ixy  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ixy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ixy OCA], [https://pdbe.org/1ixy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ixy RCSB], [https://www.ebi.ac.uk/pdbsum/1ixy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ixy ProSAT]</span></td></tr>
 
</table>
'''Ternary complex of T4 phage BGT with UDP and a 13 mer DNA duplex'''
== 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.
 
<div style="background-color:#fffaf0;">
==Overview==
== Publication Abstract from PubMed ==
T4 phage beta-glucosyltransferase (BGT) modifies T4 DNA. We crystallized BGT with UDP-glucose and a 13mer DNA fragment containing an abasic site. We obtained two crystal structures of a ternary complex BGT-UDP-DNA at 1.8A and 2.5A resolution, one with a Tris molecule and the other with a metal ion at the active site. Both structures reveal a large distortion in the bound DNA. BGT flips the deoxyribose moiety at the abasic site to an extra-helical position and induces a 40 degrees bend in the DNA with a marked widening of the major groove. The Tris molecule mimics the glucose moiety in its transition state. The base-flipping mechanism, which has so far been observed only for glycosylases, methyltransferases and endonucleases, is now reported for a glucosyltransferase. BGT is unique in binding and inserting a loop into the DNA duplex through the major groove only. Furthermore, BGT compresses the backbone DNA one base further than the target base on the 3'-side.
T4 phage beta-glucosyltransferase (BGT) modifies T4 DNA. We crystallized BGT with UDP-glucose and a 13mer DNA fragment containing an abasic site. We obtained two crystal structures of a ternary complex BGT-UDP-DNA at 1.8A and 2.5A resolution, one with a Tris molecule and the other with a metal ion at the active site. Both structures reveal a large distortion in the bound DNA. BGT flips the deoxyribose moiety at the abasic site to an extra-helical position and induces a 40 degrees bend in the DNA with a marked widening of the major groove. The Tris molecule mimics the glucose moiety in its transition state. The base-flipping mechanism, which has so far been observed only for glycosylases, methyltransferases and endonucleases, is now reported for a glucosyltransferase. BGT is unique in binding and inserting a loop into the DNA duplex through the major groove only. Furthermore, BGT compresses the backbone DNA one base further than the target base on the 3'-side.


==About this Structure==
A base-flipping mechanism for the T4 phage beta-glucosyltransferase and identification of a transition-state analog.,Lariviere L, Morera S J Mol Biol. 2002 Nov 29;324(3):483-90. PMID:12445783<ref>PMID:12445783</ref>
1IXY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IXY OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
A base-flipping mechanism for the T4 phage beta-glucosyltransferase and identification of a transition-state analog., Lariviere L, Morera S, J Mol Biol. 2002 Nov 29;324(3):483-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12445783 12445783]
</div>
[[Category: DNA beta-glucosyltransferase]]
<div class="pdbe-citations 1ixy" style="background-color:#fffaf0;"></div>
[[Category: Enterobacteria phage t4]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Lariviere, L.]]
__TOC__
[[Category: Morera, S.]]
</StructureSection>
[[Category: Abasic site]]
[[Category: Escherichia virus T4]]
[[Category: Base-flipping]]
[[Category: Large Structures]]
[[Category: Protein-dna complex]]
[[Category: Lariviere L]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:33:49 2008''
[[Category: Morera S]]

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