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==Crystal structure of the metallo-beta-lactamase fold protein YhfI from Bacillus subtilis (space group P4332)==
<StructureSection load='6knt' size='340' side='right'caption='[[6knt]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6knt]] is a 4 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=6KNT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KNT 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6knt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6knt OCA], [https://pdbe.org/6knt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6knt RCSB], [https://www.ebi.ac.uk/pdbsum/6knt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6knt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E0TYN8_BACSH E0TYN8_BACSH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Metallo-beta-lactamase (MBL) fold proteins play critical roles in diverse biological processes, such as DNA repair, RNA processing, detoxification, and metabolism. Although MBL fold proteins share a metal-bound alphabetabetaalpha structure, they are highly heterogeneous in metal type, metal coordination, and oligomerization and exhibit different catalytic functions. Bacillus subtilis contains the yhfI gene, which is predicted to encode an MBL fold protein. To reveal the structural and functional features of YhfI, we determined two crystal structures of YhfI and biochemically characterized the catalytic activity of YhfI. YhfI forms an alpha-helix-decorated beta-sandwich structure and assembles into a dimer using highly conserved residues. Each YhfI chain simultaneously interacts with two metal ions, which are coordinated by histidine and aspartate residues that are strictly conserved in YhfI orthologs. A comparative analysis of YhfI and its homologous structures suggests that YhfI would function as a phosphodiesterase. Indeed, YhfI drove the phosphodiesterase reaction and showed high catalytic activity at pH 8.0-9.5 in the presence of manganese. Moreover, we propose that the active site of YhfI is located at a metal-containing pocket generated between the two subunits of a YhfI dimer.

Structural and biochemical analyses of the metallo-beta-lactamase fold protein YhfI from Bacillus subtilis.,Na HW, Namgung B, Song WS, Yoon SI Biochem Biophys Res Commun. 2019 Oct 29;519(1):35-40. doi:, 10.1016/j.bbrc.2019.08.106. Epub 2019 Aug 31. PMID:31481231<ref>PMID:31481231</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6knt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Na HW]]
[[Category: Namgung B]]
[[Category: Song WS]]
[[Category: Yoon SI]]