1ex2

From Proteopedia

(Difference between revisions)

Current revision

CRYSTAL STRUCTURE OF BACILLUS SUBTILIS MAF PROTEIN

Structural highlights

1ex2 is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ex2"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ex2' size='340' side='right'caption='[[1ex2]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ex2]] is a 2 chain structure with sequence from [https://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=1EX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EX2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ex2]] 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=1EX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EX2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=FRU:FRUCTOSE'>FRU</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]] 1.85&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1ex2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ex2 OCA], [https://pdbe.org/1ex2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ex2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ex2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ex2 ProSAT], [https://www.topsan.org/Proteins/MCSG/1ex2 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[https://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ex/1ex2_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>
   </jmolCheckbox>
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Vibrio subtilis ehrenberg 1835]]
+[[Category: Bacillus subtilis]]
 [[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 protein maf]]
-[[Category: Mcsg]]
-[[Category: PSI, Protein structure initiative]]

1ex2

From Proteopedia

Current revision

CRYSTAL STRUCTURE OF BACILLUS SUBTILIS MAF PROTEIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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