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1sxp
From Proteopedia
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[[Image:1sxp.gif|left|200px]] | [[Image:1sxp.gif|left|200px]] | ||
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'''BGT in complex with a 13mer DNA containing a central A:G mismatch''' | '''BGT in complex with a 13mer DNA containing a central A:G mismatch''' | ||
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[[Category: Lariviere, L.]] | [[Category: Lariviere, L.]] | ||
[[Category: Morera, S.]] | [[Category: Morera, S.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:15:22 2008'' | |
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Revision as of 06:15, 3 May 2008
BGT in complex with a 13mer DNA containing a central A:G mismatch
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
1SXP 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 Sat May 3 09:15:22 2008
