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6n06

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==Cryo-EM structure of the HO BMC shell: BMC-T1 in the assembled shell==
==Cryo-EM structure of the HO BMC shell: BMC-T1 in the assembled shell==
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<StructureSection load='6n06' size='340' side='right'caption='[[6n06]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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<SX load='6n06' size='340' side='right' viewer='molstar' caption='[[6n06]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6n06]] is a 39 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=6N06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N06 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6n06]] is a 39 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=6N06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N06 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hoch_5812 ([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])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<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=6n06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n06 OCA], [http://pdbe.org/6n06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n06 RCSB], [http://www.ebi.ac.uk/pdbsum/6n06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n06 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6n06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n06 OCA], [https://pdbe.org/6n06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n06 RCSB], [https://www.ebi.ac.uk/pdbsum/6n06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n06 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/BMCT1_HALO1 BMCT1_HALO1] A minor component 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 40 nm artificial BMCs with a molecular mass of 6.5 MDa. This protein does not form stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of BMC-T trimers protruding to the exterior.<ref>PMID:28642439</ref> <ref>PMID:30833088</ref>
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6n06" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Halo1]]
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[[Category: Haliangium ochraceum DSM 14365]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Greber, B J]]
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[[Category: Greber BJ]]
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[[Category: Kerfeld, C A]]
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[[Category: Kerfeld CA]]
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[[Category: Sutter, M]]
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[[Category: Sutter M]]
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[[Category: Bmc fold]]
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[[Category: Compartmentalization]]
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[[Category: Microcompartment]]
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[[Category: Shell]]
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[[Category: Structural protein]]
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Current revision

Cryo-EM structure of the HO BMC shell: BMC-T1 in the assembled shell

6n06, resolution 3.40Å

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