4heb: Difference between revisions
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==The Crystal structure of Maf protein of Bacillus subtilis== | ||
[[http://www.uniprot.org/uniprot/ | <StructureSection load='4heb' size='340' side='right'caption='[[4heb]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4heb]] 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=4HEB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26Å</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=4heb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4heb OCA], [https://pdbe.org/4heb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4heb RCSB], [https://www.ebi.ac.uk/pdbsum/4heb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4heb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Maf (for multicopy associated filamentation) proteins represent a large family of conserved proteins implicated in cell division arrest but whose biochemical activity remains unknown. Here, we show that the prokaryotic and eukaryotic Maf proteins exhibit nucleotide pyrophosphatase activity against 5-methyl-UTP, pseudo-UTP, 5-methyl-CTP, and 7-methyl-GTP, which represent the most abundant modified bases in all organisms, as well as against canonical nucleotides dTTP, UTP, and CTP. Overexpression of the Maf protein YhdE in E. coli cells increased intracellular levels of dTMP and UMP, confirming that dTTP and UTP are the in vivo substrates of this protein. Crystal structures and site-directed mutagenesis of Maf proteins revealed the determinants of their activity and substrate specificity. Thus, pyrophosphatase activity of Maf proteins toward canonical and modified nucleotides might provide the molecular mechanism for a dual role of these proteins in cell division arrest and house cleaning. | |||
Biochemical and Structural Studies of Conserved Maf Proteins Revealed Nucleotide Pyrophosphatases with a Preference for Modified Nucleotides.,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 Chem Biol. 2013 Oct 22. pii: S1074-5521(13)00347-5. doi:, 10.1016/j.chembiol.2013.09.011. PMID:24210219<ref>PMID:24210219</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[Category: Bacillus | <div class="pdbe-citations 4heb" style="background-color:#fffaf0;"></div> | ||
[[Category: Arrowsmith | == References == | ||
[[Category: Bountra | <references/> | ||
[[Category: Brown | __TOC__ | ||
[[Category: Dombrovski | </StructureSection> | ||
[[Category: Dong | [[Category: Bacillus subtilis]] | ||
[[Category: Edwards | [[Category: Large Structures]] | ||
[[Category: Flick | [[Category: Arrowsmith CH]] | ||
[[Category: Iakounine | [[Category: Bountra C]] | ||
[[Category: Min | [[Category: Brown G]] | ||
[[Category: Dombrovski L]] | |||
[[Category: Tchigvintsev | [[Category: Dong A]] | ||
[[Category: Wu | [[Category: Edwards AM]] | ||
[[Category: Flick R]] | |||
[[Category: Iakounine A]] | |||
[[Category: Min J]] | |||
[[Category: Tchigvintsev D]] | |||
[[Category: Wu H]] | |||
Latest revision as of 13:04, 30 October 2024
The Crystal structure of Maf protein of Bacillus subtilisThe Crystal structure of Maf protein of Bacillus subtilis
Structural highlights
FunctionNTPPA_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] Publication Abstract from PubMedMaf (for multicopy associated filamentation) proteins represent a large family of conserved proteins implicated in cell division arrest but whose biochemical activity remains unknown. Here, we show that the prokaryotic and eukaryotic Maf proteins exhibit nucleotide pyrophosphatase activity against 5-methyl-UTP, pseudo-UTP, 5-methyl-CTP, and 7-methyl-GTP, which represent the most abundant modified bases in all organisms, as well as against canonical nucleotides dTTP, UTP, and CTP. Overexpression of the Maf protein YhdE in E. coli cells increased intracellular levels of dTMP and UMP, confirming that dTTP and UTP are the in vivo substrates of this protein. Crystal structures and site-directed mutagenesis of Maf proteins revealed the determinants of their activity and substrate specificity. Thus, pyrophosphatase activity of Maf proteins toward canonical and modified nucleotides might provide the molecular mechanism for a dual role of these proteins in cell division arrest and house cleaning. Biochemical and Structural Studies of Conserved Maf Proteins Revealed Nucleotide Pyrophosphatases with a Preference for Modified Nucleotides.,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 Chem Biol. 2013 Oct 22. pii: S1074-5521(13)00347-5. doi:, 10.1016/j.chembiol.2013.09.011. PMID:24210219[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||