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3h6d

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Revision as of 05:20, 7 December 2018

Structure of the mycobacterium tuberculosis DUTPase D28N mutant

Structural highlights

3h6d is a 1 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	dut, MT2771, MTCY05A6.18c, Rv2697c ("Bacillus tuberculosis" (Zopf 1883) Klein 1884)
Activity:	dUTP diphosphatase, with EC number 3.6.1.23
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DUT_MYCTU] This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.[HAMAP-Rule:MF_00116]

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

dUTP pyrophosphatases (dUTPases) are essential for genome integrity. Recent results allowed characterization of the role of conserved residues. Here we analyzed the Asp/Asn mutation within conserved Motif I of human and mycobacterial dUTPases, wherein the Asp residue was previously implicated in Mg(2+)-coordination. Our results on transient/steady-state kinetics, ligand binding and a 1.80 A resolution structure of the mutant mycobacterial enzyme, in comparison with wild type and C-terminally truncated structures, argue that this residue has a major role in providing intra- and intersubunit contacts, but is not essential for Mg(2+) accommodation. We conclude that in addition to the role of conserved motifs in substrate accommodation, direct subunit interaction between protein atoms of active site residues from different conserved motifs are crucial for enzyme function.

Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases.,Takacs E, Nagy G, Leveles I, Harmat V, Lopata A, Toth J, Vertessy BG FEBS Lett. 2010 Jul 16;584(14):3047-54. Epub 2010 May 21. PMID:20493855^[1]

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

References

↑ Takacs E, Nagy G, Leveles I, Harmat V, Lopata A, Toth J, Vertessy BG. Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases. FEBS Lett. 2010 Jul 16;584(14):3047-54. Epub 2010 May 21. PMID:20493855 doi:10.1016/j.febslet.2010.05.018

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/3h6d"

@@ Line 1: / Line 1: @@
 ==Structure of the mycobacterium tuberculosis DUTPase D28N mutant==
 <StructureSection load='3h6d' size='340' side='right' caption='[[3h6d]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dut, MT2771, MTCY05A6.18c, Rv2697c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] </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=3h6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h6d OCA], [http://pdbe.org/3h6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h6d RCSB], [http://www.ebi.ac.uk/pdbsum/3h6d PDBsum]</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=3h6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h6d OCA], [http://pdbe.org/3h6d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h6d RCSB], [http://www.ebi.ac.uk/pdbsum/3h6d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h6d ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/3h6d_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/3h6d_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

3h6d

From Proteopedia

Revision as of 05:20, 7 December 2018

Structure of the mycobacterium tuberculosis DUTPase D28N mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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