1jg6: Difference between revisions
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'''T4 phage BGT in complex with UDP''' | {{Structure | ||
|PDB= 1jg6 |SIZE=350|CAPTION= <scene name='initialview01'>1jg6</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</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= | |||
}} | |||
'''T4 phage BGT in complex with UDP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JG6 is a [ | 1JG6 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=1JG6 OCA]. | ||
==Reference== | ==Reference== | ||
High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding., Morera S, Lariviere L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Ruger W, J Mol Biol. 2001 Aug 17;311(3):569-77. PMID:[http:// | High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding., Morera S, Lariviere L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Ruger W, J Mol Biol. 2001 Aug 17;311(3):569-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11493010 11493010] | ||
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: DNA beta-glucosyltransferase]] | [[Category: DNA beta-glucosyltransferase]] | ||
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[[Category: glycosyltransferase]] | [[Category: glycosyltransferase]] | ||
''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 12:02:59 2008'' | ||
Revision as of 13:03, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | |||||||
| Activity: | DNA beta-glucosyltransferase, with EC number 2.4.1.27 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
T4 phage BGT in complex with UDP
OverviewOverview
beta-Glucosyltransferase (BGT) is a DNA-modifying enzyme encoded by bacteriophage T4 that transfers glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine bases of phage T4 DNA. We report six X-ray structures of the substrate-free and the UDP-bound enzyme. Four also contain metal ions which activate the enzyme, including Mg(2+) in forms 1 and 2 and Mn(2+) or Ca(2+). The substrate-free BGT structure differs by a domain movement from one previously determined in another space group. Further domain movements are seen in the complex with UDP and the four UDP-metal complexes. Mg(2+), Mn(2+) and Ca(2+) bind near the beta-phosphate of the nucleotide, but they occupy slightly different positions and have different ligands depending on the metal and the crystal form. Whilst the metal site observed in these complexes with the product UDP is not compatible with a role in activating glucose transfer, it approximates the position of the positive charge in the oxocarbonium ion thought to form on the glucose moiety of the substrate during catalysis.
About this StructureAbout this Structure
1JG6 is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
ReferenceReference
High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding., Morera S, Lariviere L, Kurzeck J, Aschke-Sonnenborn U, Freemont PS, Janin J, Ruger W, J Mol Biol. 2001 Aug 17;311(3):569-77. PMID:11493010
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