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2zhx

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{{STRUCTURE_2zhx| PDB=2zhx | SCENE= }}
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'''Crystal structure of Uracil-DNA Glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor'''
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===Crystal structure of Uracil-DNA Glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor===
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==Overview==
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Uracil-DNA glycosylase (UNG), a repair enzyme involved in the excision of uracil from DNA, from mycobacteria differs from UNGs from other sources, particularly in the sequence in the catalytically important loops. The structure of the enzyme from Mycobacterium tuberculosis (MtUng) in complex with a proteinaceous inhibitor (Ugi) has been determined by X-ray analysis of a crystal containing seven crystallographically independent copies of the complex. This structure provides the first geometric characterization of a mycobacterial UNG. A comparison of the structure with those of other UNG proteins of known structure shows that a central core region of the molecule is relatively invariant in structure and sequence, while the N- and C-terminal tails exhibit high variability. The tails are probably important in folding and stability. The mycobacterial enzyme exhibits differences in UNG-Ugi interactions compared with those involving UNG from other sources. The MtUng-DNA complex modelled on the basis of the known structure of the complex involving the human enzyme indicates a domain closure in the enzyme when binding to DNA. The binding involves a larger burial of surface area than is observed in binding by human UNG. The DNA-binding site of MtUng is characterized by the presence of a higher proportion of arginyl residues than is found in the binding site of any other UNG of known structure. In addition to the electrostatic effects produced by the arginyl residues, the hydrogen bonds in which they are involved compensate for the loss of some interactions arising from changes in amino-acid residues, particularly in the catalytic loops. The results arising from the present investigation represent unique features of the structure and interaction of mycobacterial Ungs.
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{{ABSTRACT_PUBMED_18453691}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources., Kaushal PS, Talawar RK, Krishna PD, Varshney U, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):551-60. Epub 2008, Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18453691 18453691]
Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources., Kaushal PS, Talawar RK, Krishna PD, Varshney U, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):551-60. Epub 2008, Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18453691 18453691]
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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://www.ncbi.nlm.nih.gov/pubmed/12136137 12136137]
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X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG., Ravishankar R, Bidya Sagar M, Roy S, Purnapatre K, Handa P, Varshney U, Vijayan M, Nucleic Acids Res. 1998 Nov 1;26(21):4880-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9776748 9776748]
[[Category: Bacillus phage pbs2]]
[[Category: Bacillus phage pbs2]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Ung-dna interaction]]
[[Category: Ung-dna interaction]]
[[Category: Ung-ugi complex]]
[[Category: Ung-ugi complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:47:22 2008''

Revision as of 21:47, 27 July 2008

Image:2zhx.png

Template:STRUCTURE 2zhx

Crystal structure of Uracil-DNA Glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor

Template:ABSTRACT PUBMED 18453691

About this Structure

2ZHX is a Protein complex structure of sequences from Bacillus phage pbs2 and Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources., Kaushal PS, Talawar RK, Krishna PD, Varshney U, Vijayan M, Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):551-60. Epub 2008, Apr 19. PMID:18453691

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

X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a prokaryotic UDG., Ravishankar R, Bidya Sagar M, Roy S, Purnapatre K, Handa P, Varshney U, Vijayan M, Nucleic Acids Res. 1998 Nov 1;26(21):4880-7. PMID:9776748

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