1lqg

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[[Image:1lqg.jpg|left|200px]]<br /><applet load="1lqg" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1lqg, resolution 2.90&Aring;" />
 
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'''ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN'''<br />
 
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==Overview==
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==ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN==
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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.
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<StructureSection load='1lqg' size='340' side='right'caption='[[1lqg]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1lqg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_PBS2 Bacillus phage PBS2] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqg OCA], [https://pdbe.org/1lqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqg RCSB], [https://www.ebi.ac.uk/pdbsum/1lqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lq/1lqg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1lqg ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1LQG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Phage_pbs1 Phage pbs1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQG OCA].
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*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
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*[[Uracil glycosylase inhibitor|Uracil glycosylase inhibitor]]
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==Reference==
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__TOC__
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12136137 12136137]
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</StructureSection>
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[[Category: Bacillus phage PBS2]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Phage pbs1]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Handa P]]
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[[Category: Handa, P.]]
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[[Category: Purnapatre K]]
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[[Category: Purnapatre, K.]]
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[[Category: Ravishankar R]]
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[[Category: Ravishankar, R.]]
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[[Category: Roy S]]
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[[Category: Roy, S.]]
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[[Category: Sagar MB]]
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[[Category: Sagar, M B.]]
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[[Category: Saikrishnan K]]
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[[Category: Saikrishnan, K.]]
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[[Category: Varshney U]]
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[[Category: Varshney, U.]]
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[[Category: Vijayan M]]
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[[Category: Vijayan, M.]]
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[[Category: base excision]]
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[[Category: complex (hydrolase/inhibitor)]]
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[[Category: dna repair]]
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[[Category: glycosylase]]
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[[Category: inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:25 2008''
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Current revision

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

PDB ID 1lqg

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