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| | <StructureSection load='1exc' size='340' side='right'caption='[[1exc]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1exc' size='340' side='right'caption='[[1exc]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1exc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EXC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1exc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DUT:DEOXYURIDINE-5-TRIPHOSPHATE'>DUT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ex2|1ex2]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DUT:DEOXYURIDINE-5-TRIPHOSPHATE'>DUT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1exc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exc OCA], [http://pdbe.org/1exc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1exc RCSB], [http://www.ebi.ac.uk/pdbsum/1exc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1exc ProSAT], [http://www.topsan.org/Proteins/MCSG/1exc TOPSAN]</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=1exc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exc OCA], [https://pdbe.org/1exc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exc RCSB], [https://www.ebi.ac.uk/pdbsum/1exc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exc ProSAT], [https://www.topsan.org/Proteins/MCSG/1exc TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAF_BACSU MAF_BACSU]] Involved in septum formation. | + | [https://www.uniprot.org/uniprot/NTPPA_BACSU NTPPA_BACSU] Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo-UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP) (PubMed:24210219). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids (PubMed:24210219).<ref>PMID:24210219</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/1exc_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/1exc_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Anderson, W F]] | + | [[Category: Anderson WF]] |
| - | [[Category: Egli, M]] | + | [[Category: Egli M]] |
| - | [[Category: Koonin, E V]] | + | [[Category: Koonin EV]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Minasov G]] |
| - | [[Category: Minasov, G]] | + | [[Category: Stewart GC]] |
| - | [[Category: Stewart, G C]] | + | [[Category: Teplova M]] |
| - | [[Category: Teplova, M]] | + | |
| - | [[Category: B subtilis maf protein complexed with dutp]]
| + | |
| - | [[Category: Mcsg]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| Structural highlights
Function
NTPPA_BACSU Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo-UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP) (PubMed:24210219). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids (PubMed:24210219).[1]
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
Three-dimensional structures of functionally uncharacterized proteins may furnish insight into their functions. The potential benefits of three-dimensional structural information regarding such proteins are particularly obvious when the corresponding genes are conserved during evolution, implying an important function, and no functional classification can be inferred from their sequences. The Bacillus subtilis Maf protein is representative of a family of proteins that has homologs in many of the completely sequenced genomes from archaea, prokaryotes, and eukaryotes, but whose function is unknown. As an aid in exploring function, we determined the crystal structure of this protein at a resolution of 1.85 A. The structure, in combination with multiple sequence alignment, reveals a putative active site. Phosphate ions present at this site and structural similarities between a portion of Maf and the anticodon-binding domains of several tRNA synthetases suggest that Maf may be a nucleic acid-binding protein. The crystal structure of a Maf-nucleoside triphosphate complex provides support for this hypothesis and hints at di- or oligonucleotides with either 5'- or 3'-terminal phosphate groups as ligands or substrates of Maf. A further clue comes from the observation that the structure of the Maf monomer bears similarity to that of the recently reported Methanococcus jannaschii Mj0226 protein. Just as for Maf, the structure of this predicted NTPase was determined as part of a structural genomics pilot project. The structural relation between Maf and Mj0226 was not apparent from sequence analysis approaches. These results emphasize the potential of structural genomics to reveal new unexpected connections between protein families previously considered unrelated.
Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP.,Minasov G, Teplova M, Stewart GC, Koonin EV, Anderson WF, Egli M Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6328-33. PMID:10841541[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tchigvintsev A, Tchigvintsev D, Flick R, Popovic A, Dong A, Xu X, Brown G, Lu W, Wu H, Cui H, Dombrowski L, Joo JC, Beloglazova N, Min J, Savchenko A, Caudy AA, Rabinowitz JD, Murzin AG, Yakunin AF. Biochemical and Structural Studies of Conserved Maf Proteins Revealed Nucleotide Pyrophosphatases with a Preference for Modified Nucleotides. Chem Biol. 2013 Oct 22. pii: S1074-5521(13)00347-5. doi:, 10.1016/j.chembiol.2013.09.011. PMID:24210219 doi:http://dx.doi.org/10.1016/j.chembiol.2013.09.011
- ↑ Minasov G, Teplova M, Stewart GC, Koonin EV, Anderson WF, Egli M. Functional implications from crystal structures of the conserved Bacillus subtilis protein Maf with and without dUTP. Proc Natl Acad Sci U S A. 2000 Jun 6;97(12):6328-33. PMID:10841541
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