4heb: Difference between revisions
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==The Crystal structure of Maf protein of Bacillus subtilis== | ==The Crystal structure of Maf protein of Bacillus subtilis== | ||
<StructureSection load='4heb' size='340' side='right' caption='[[4heb]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='4heb' size='340' side='right' caption='[[4heb]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p5x|2p5x]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p5x|2p5x]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">maf, BSU28050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">maf, BSU28050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=4heb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4heb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4heb RCSB], [http://www.ebi.ac.uk/pdbsum/4heb 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=4heb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4heb OCA], [http://pdbe.org/4heb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4heb RCSB], [http://www.ebi.ac.uk/pdbsum/4heb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4heb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4heb" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 12:54, 4 August 2016
The Crystal structure of Maf protein of Bacillus subtilisThe Crystal structure of Maf protein of Bacillus subtilis
Structural highlights
Function[MAF_BACSU] Involved in septum formation. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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