1ixy
From Proteopedia
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| - | [[Image:1ixy.gif|left|200px]] | + | [[Image:1ixy.gif|left|200px]] |
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| - | '''Ternary complex of T4 phage BGT with UDP and a 13 mer DNA duplex''' | + | {{Structure |
| + | |PDB= 1ixy |SIZE=350|CAPTION= <scene name='initialview01'>1ixy</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
| + | |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] | ||
| + | |GENE= BGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage T4]) | ||
| + | }} | ||
| + | |||
| + | '''Ternary complex of T4 phage BGT with UDP and a 13 mer DNA duplex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IXY is a [ | + | 1IXY 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=1IXY OCA]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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] |
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: DNA beta-glucosyltransferase]] | [[Category: DNA beta-glucosyltransferase]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:56:22 2008'' |
Revision as of 09:56, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | BGT (Bacteriophage T4) | ||||||
| Activity: | DNA beta-glucosyltransferase, with EC number 2.4.1.27 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ternary complex of T4 phage BGT with UDP and a 13 mer DNA duplex
Overview
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
1IXY is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:56:22 2008
