1lqm
From Proteopedia
(New page: 200px<br /><applet load="1lqm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lqm, resolution 3.20Å" /> '''ESCHERICHIA COLI URA...) |
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| - | [[Image:1lqm.jpg|left|200px]]<br /><applet load="1lqm" size=" | + | [[Image:1lqm.jpg|left|200px]]<br /><applet load="1lqm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lqm, resolution 3.20Å" /> | caption="1lqm, resolution 3.20Å" /> | ||
'''ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN'''<br /> | '''ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of a new crystal form of free Escherichia coli uracil DNA | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1LQM 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:// | + | 1LQM 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=1LQM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ravishankar, R.]] | [[Category: Ravishankar, R.]] | ||
[[Category: Roy, S.]] | [[Category: Roy, S.]] | ||
| - | [[Category: Sagar, M | + | [[Category: Sagar, M B.]] |
[[Category: Saikrishnan, K.]] | [[Category: Saikrishnan, K.]] | ||
[[Category: Varshney, U.]] | [[Category: Varshney, U.]] | ||
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[[Category: inhibitor]] | [[Category: inhibitor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:31 2008'' |
Revision as of 11:47, 21 February 2008
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ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN
Overview
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.
About this Structure
1LQM is a Protein complex structure of sequences from Escherichia coli and Phage pbs1. Full crystallographic information is available from OCA.
Reference
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
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