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==Cryo-EM structure of the HO BMC shell: Icosahedral reconstruction of the compacted subpopulation==
==Cryo-EM structure of the HO BMC shell: Icosahedral reconstruction of the compacted subpopulation==
<StructureSection load='6mzy' size='340' side='right'caption='[[6mzy]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<SX load='6mzy' size='340' side='right' viewer='molstar' caption='[[6mzy]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6mzy]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Halo1 Halo1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MZY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MZY FirstGlance]. <br>
<table><tr><td colspan='2'>[[6mzy]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliangium_ochraceum_DSM_14365 Haliangium ochraceum DSM 14365]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MZY FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mzu|6mzu]], [[6mzv|6mzv]], [[6mzx|6mzx]], [[6n06|6n06]], [[6n07|6n07]], [[6n09|6n09]], [[6n0f|6n0f]], [[6n0g|6n0g]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hoch_5814 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502025 HALO1]), Hoch_5815 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502025 HALO1]), Hoch_5816 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=502025 HALO1])</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=6mzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzy OCA], [https://pdbe.org/6mzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mzy RCSB], [https://www.ebi.ac.uk/pdbsum/6mzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzy ProSAT]</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=6mzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzy OCA], [http://pdbe.org/6mzy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mzy RCSB], [http://www.ebi.ac.uk/pdbsum/6mzy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzy ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/BMCH_HALO1 BMCH_HALO1] The only hexameric shell protein in this bacterium, it forms the majority of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms a 40 nm artificial BMC with a molecular mass of 6.5 MDa. There are 60 BMC-H hexamers per BMC. The shell facets are 20-30 Angstroms thick (a single hexamer layer), with 1 of BMC-T trimers protruding to the exterior.<ref>PMID:28642439</ref> <ref>PMID:30833088</ref>  
Bacterial microcompartments (BMCs) are composed of an enzymatic core encapsulated by a selectively permeable protein shell that enhances catalytic efficiency. Many pathogenic bacteria derive competitive advantages from their BMC-based catabolism, implicating BMCs as drug targets. BMC shells are of interest for bioengineering due to their diverse and selective permeability properties and because they self-assemble. A complete understanding of shell composition and organization is a prerequisite for biotechnological applications. Here, we report the cryoelectron microscopy structure of a BMC shell at 3.0-A resolution, using an image-processing strategy that allowed us to determine the previously uncharacterized structural details of the interactions formed by the BMC-T(S) and BMC-T(D) shell subunits in the context of the assembled shell. We found unexpected structural plasticity among these interactions, resulting in distinct shell populations assembled from varying numbers of the BMC-T(S) and BMC-T(D) subunits. We discuss the implications of these findings on shell assembly and function.
 
The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly.,Greber BJ, Sutter M, Kerfeld CA Structure. 2019 Feb 12. pii: S0969-2126(19)30017-6. doi:, 10.1016/j.str.2019.01.017. PMID:30833088<ref>PMID:30833088</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6mzy" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Halo1]]
[[Category: Haliangium ochraceum DSM 14365]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Greber, B J]]
[[Category: Greber BJ]]
[[Category: Kerfeld, C A]]
[[Category: Kerfeld CA]]
[[Category: Sutter, M]]
[[Category: Sutter M]]
[[Category: Bmc fold]]
[[Category: Compartmentalization]]
[[Category: Microcompartment]]
[[Category: Shell]]
[[Category: Structural protein]]
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