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2zhx

From Proteopedia

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

Structural highlights

2zhx is a 14 chain structure with sequence from Bacillus phage PBS2 and Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UNG_MYCTU 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 (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kaushal PS, Talawar RK, Krishna PD, Varshney U, Vijayan M. 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. Acta Crystallogr D Biol Crystallogr. 2008 May;64(Pt 5):551-60. Epub 2008, Apr 19. PMID:18453691 doi:10.1107/S090744490800512X

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zhx"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Uracil-DNA Glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor==
-<StructureSection load='2zhx' size='340' side='right' caption='[[2zhx]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='2zhx' size='340' side='right'caption='[[2zhx]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2zhx]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_pbs2 Bacteriophage pbs2] and [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZHX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2zhx]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_PBS2 Bacillus phage PBS2] and [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZHX FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ung, Rv2976c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]), ugi, J04434 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Bacteriophage PBS2])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_nucleosidase Uridine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.3 3.2.2.3] </span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zhx OCA], [https://pdbe.org/2zhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zhx RCSB], [https://www.ebi.ac.uk/pdbsum/2zhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zhx ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zhx OCA], [http://pdbe.org/2zhx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zhx RCSB], [http://www.ebi.ac.uk/pdbsum/2zhx PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/UNG_MYCTU UNG_MYCTU]] 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 (By similarity). [[http://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.
+[https://www.uniprot.org/uniprot/UNG_MYCTU UNG_MYCTU] 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 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zh/2zhx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zh/2zhx_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[DNA glycosylase|DNA glycosylase]]
+*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
-*[[Uracil glycosylate inhibitor|Uracil glycosylate inhibitor]]
+*[[Uracil glycosylase inhibitor|Uracil glycosylase inhibitor]]
-*[[Uracil-DNA glycosylase|Uracil-DNA glycosylase]]
-*[[Uracil-DNA glycosylase inhibitor|Uracil-DNA glycosylase inhibitor]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bacteriophage pbs2]]
+[[Category: Bacillus phage PBS2]]
-[[Category: Mycobacterium tuberculosis]]
+[[Category: Large Structures]]
-[[Category: Uridine nucleosidase]]
+[[Category: Mycobacterium tuberculosis H37Rv]]
-[[Category: Kaushal, P S]]
+[[Category: Kaushal PS]]
-[[Category: Krishna, P D.V]]
+[[Category: Krishna PDV]]
-[[Category: Talawar, R K]]
+[[Category: Talawar RK]]
-[[Category: Varshney, U]]
+[[Category: Varshney U]]
-[[Category: Vijayan, M]]
+[[Category: Vijayan M]]
-[[Category: Dna damage]]
-[[Category: Dna repair]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Ung-dna interaction]]
-[[Category: Ung-ugi complex]]

2zhx

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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