1sxq
From Proteopedia
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|PDB= 1sxq |SIZE=350|CAPTION= <scene name='initialview01'>1sxq</scene>, resolution 1.8Å | |PDB= 1sxq |SIZE=350|CAPTION= <scene name='initialview01'>1sxq</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene> | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
| - | |GENE= BGT, BETA-GT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | |GENE= BGT, BETA-GT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4]) |
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1m5r|1M5R]], [[1ixy|1IXY]], [[1sxp|1SXP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sxq OCA], [http://www.ebi.ac.uk/pdbsum/1sxq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sxq RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SXQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1SXQ 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=1SXQ OCA]. |
==Reference== | ==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] | 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: DNA beta-glucosyltransferase]] | ||
| + | [[Category: Enterobacteria phage t4]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lariviere, L.]] | [[Category: Lariviere, L.]] | ||
[[Category: Morera, S.]] | [[Category: Morera, S.]] | ||
| - | [[Category: UDP]] | ||
[[Category: flipped-out base]] | [[Category: flipped-out base]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:48:23 2008'' |
Revision as of 20:48, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Gene: | BGT, BETA-GT (Enterobacteria phage T4) | ||||||
| Activity: | DNA beta-glucosyltransferase, with EC number 2.4.1.27 | ||||||
| Related: | 1M5R, 1IXY, 1SXP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BGT in complex with a 13mer DNA containing a central C:G base pair and UDP
Overview
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.
About this Structure
1SXQ is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
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:15178685
Page seeded by OCA on Sun Mar 30 23:48:23 2008
