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1sxp

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[[Image:1sxp.gif|left|200px]]
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{{STRUCTURE_1sxp| PDB=1sxp | SCENE= }}
{{STRUCTURE_1sxp| PDB=1sxp | SCENE= }}
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'''BGT in complex with a 13mer DNA containing a central A:G mismatch'''
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===BGT in complex with a 13mer DNA containing a central A:G mismatch===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15178685 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15178685}}
==About this Structure==
==About this Structure==
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[[Category: Morera, S.]]
[[Category: Morera, S.]]
[[Category: Flipped-out base]]
[[Category: Flipped-out base]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:25:44 2008''

Revision as of 12:25, 29 July 2008

Template:STRUCTURE 1sxp

BGT in complex with a 13mer DNA containing a central A:G mismatch

Template:ABSTRACT PUBMED 15178685

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

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