View source for 9bxa


==Structure of Mnx H340A complex from Bacillus sp. PL-12==
<StructureSection load='9bxa' size='340' side='right'caption='[[9bxa]], [[Resolution|resolution]] 3.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9bxa]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._(in:_Bacteria) Bacillus sp. (in: Bacteria)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BXA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.37&#8491;</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=9bxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bxa OCA], [https://pdbe.org/9bxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bxa RCSB], [https://www.ebi.ac.uk/pdbsum/9bxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bxa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A7KBU7_9BACI A7KBU7_9BACI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The global manganese cycle relies on microbes to oxidize soluble Mn(II) to insoluble Mn(IV) oxides. Some microbes require peroxide or superoxide as oxidants, but others can use O(2) directly, via multicopper oxidase (MCO) enzymes. One of these, MnxG from Bacillus sp. strain PL-12, was isolated in tight association with small accessory proteins, MnxE and MnxF. The protein complex, called Mnx, has eluded crystallization efforts, but we now report the 3D structure of a point mutant using cryo-EM single particle analysis, cross-linking mass spectrometry, and AlphaFold Multimer prediction. The beta-sheet-rich complex features MnxG enzyme, capped by a heterohexameric ring of alternating MnxE and MnxF subunits, and a tunnel that runs through MnxG and its MnxE(3)F(3) cap. The tunnel dimensions and charges can accommodate the mechanistically inferred binuclear manganese intermediates. Comparison with the Fe(II)-oxidizing MCO, ceruloplasmin, identifies likely coordinating groups for the Mn(II) substrate, at the entrance to the tunnel. Thus, the 3D structure provides a rationale for the established manganese oxidase mechanism, and a platform for further experiments to elucidate mechanistic details of manganese biomineralization.

Cryo-EM Structure of the Mnx Protein Complex Reveals a Tunnel Framework for the Mechanism of Manganese Biomineralization.,Novikova IV, Soldatova AV, Moser TH, Thibert SM, Romano CA, Zhou M, Tebo BM, Evans JE, Spiro TG J Am Chem Soc. 2024 Jul 26. doi: 10.1021/jacs.3c06537. PMID:39056168<ref>PMID:39056168</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9bxa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Evans JE]]
[[Category: Novikova IV]]