1lqg

<table><tr><td colspan='2'>[[1lqg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [https://en.wikipedia.org/wiki/Bppb2 Bppb2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQG FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eui|1eui]], [[1lqj|1lqj]], [[1lqm|1lqm]]</div></td></tr>

[[https://www.uniprot.org/uniprot/UNG_ECOLI UNG_ECOLI]] Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.[HAMAP-Rule:MF_00148] [[https://www.uniprot.org/uniprot/UNGI_BPPB2 UNGI_BPPB2]] This protein binds specifically and reversibly to the host uracil-DNA glycosylase, preventing removal of uracil residues from PBS2 DNA by the host uracil-excision repair system.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The structures of a new crystal form of free Escherichia coli uracil DNA glycosylase (UDG), containing four molecules in the asymmetric unit, and two forms of its complex with the proteinaceous inhibitor Ugi, containing two and four crystallographically independent complexes, have been determined. A comparison of these structures and the already known crystal structures containing UDG shows that the enzyme can be considered to be made up of two independently moving structural entities or domains. A detailed study of free and DNA-bound human enzyme strengthens this conclusion. The domains close upon binding to uracil-containing DNA, whereas they do not appear to do so upon binding to Ugi. The comparative study also shows that the mobility of the molecule involves the rigid-body movement of the domains superposed on flexibility within domains.

Domain closure and action of uracil DNA glycosylase (UDG): structures of new crystal forms containing the Escherichia coli enzyme and a comparative study of the known structures involving UDG.,Saikrishnan K, Bidya Sagar M, Ravishankar R, Roy S, Purnapatre K, Handa P, Varshney U, Vijayan M Acta Crystallogr D Biol Crystallogr. 2002 Aug;58(Pt 8):1269-76. Epub 2002, Jul 20. PMID:12136137<ref>PMID:12136137</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1lqg" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Bppb2]]

[[Category: Handa, P]]

[[Category: Purnapatre, K]]

[[Category: Ravishankar, R]]

[[Category: Roy, S]]

[[Category: Sagar, M B]]

[[Category: Saikrishnan, K]]

[[Category: Varshney, U]]

[[Category: Vijayan, M]]

[[Category: Inhibitor]]