1lqm

<StructureSection load='1lqm' size='340' side='right' caption='[[1lqm]], [[Resolution|resolution]] 3.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1lqm]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_phage_pbs2 Bacillus phage pbs2] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LQM FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eui|1eui]], [[1lqg|1lqg]], [[1lqj|1lqj]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lqm RCSB], [http://www.ebi.ac.uk/pdbsum/1lqm PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lq/1lqm_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

<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>

*[[DNA glycosylase|DNA glycosylase]]

*[[Uracil glycosylate inhibitor|Uracil glycosylate inhibitor]]

*[[Uracil-DNA glycosylase inhibitor|Uracil-DNA glycosylase inhibitor]]

[[Category: Bacillus phage pbs2]]

[[Category: Purnapatre, K.]]

[[Category: Ravishankar, R.]]

[[Category: Roy, S.]]

[[Category: Sagar, M B.]]

[[Category: Saikrishnan, K.]]

[[Category: Varshney, U.]]

[[Category: Vijayan, M.]]

[[Category: Inhibitor]]