5ie9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the Bacillus-conserved MazG protein, a nucleotide pyrophosphohydrolase== | |
| + | <StructureSection load='5ie9' size='340' side='right' caption='[[5ie9]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ie9]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IE9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5ie9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ie9 OCA], [http://pdbe.org/5ie9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ie9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ie9 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BA1544 from Bacillus anthracis was previously annotated as a transcription factor for the gene cluster ba1554 - ba1558, but has not been experimentally characterized. B. anthracis is an obligate pathogen causing fatal inhalational anthrax, and BA1544 is absolutely conserved in Bacillus species, including Bacillus cereus, Bacillus thuringiensis and Bacillus mycoides, with 100% sequence identity. To address the function of BA1544, we performed structural and biochemical studies, which revealed that BA1544 is a MazG protein. Thus, herein, the protein is defined as Bacillus-conserved MazG (BcMazG). Like other MazG structures, BcMazG assembles into a tetrameric architecture. Each monomer adopts a four-alpha-helix bundle that accommodates a metal ion using four acidic residues, and presents one putative substrate-binding site. Enzymatic characterization demonstrated that BcMazG is a nucleoside triphosphate (NTP) pyrophosphohydrolase and prefers adenosine triphosphate as a substrate among canonical NTPs. Moreover, structural comparison of BcMazG with its homologues revealed a potential regulation mechanism whereby the enzymatic activity of BcMazG is regulated by its C-terminal region. | ||
| - | + | Crystal structure of the Bacillus-conserved MazG protein, a nucleotide pyrophosphohydrolase.,Kim MI, Hong M Biochem Biophys Res Commun. 2016 Mar 25;472(1):237-42. doi:, 10.1016/j.bbrc.2016.02.097. Epub 2016 Feb 23. PMID:26920050<ref>PMID:26920050</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5ie9" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hong, M]] | ||
| + | [[Category: Kim, M]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Mazg]] | ||
| + | [[Category: Nucleoside triphosphate pyrophosphohydrolase]] | ||
Revision as of 20:37, 11 May 2016
Crystal structure of the Bacillus-conserved MazG protein, a nucleotide pyrophosphohydrolase
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