1sxq: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1sxq.gif|left|200px]]
{{Seed}}
[[Image:1sxq.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1sxq|  PDB=1sxq  |  SCENE=  }}  
{{STRUCTURE_1sxq|  PDB=1sxq  |  SCENE=  }}  


'''BGT in complex with a 13mer DNA containing a central C:G base pair and UDP'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_15178685}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15178685 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15178685}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Morera, S.]]
[[Category: Morera, S.]]
[[Category: Flipped-out base]]
[[Category: Flipped-out base]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:15:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:43:09 2008''

Revision as of 16:43, 28 July 2008

File:1sxq.png

Template:STRUCTURE 1sxq

BGT in complex with a 13mer DNA containing a central C:G base pair and UDP

Template:ABSTRACT PUBMED 15178685

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 Mon Jul 28 19:43:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1sxq&oldid=712621"