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| | <SX load='6mzv' size='340' side='right' viewer='molstar' caption='[[6mzv]], [[Resolution|resolution]] 3.40Å' scene=''> | | <SX load='6mzv' size='340' side='right' viewer='molstar' caption='[[6mzv]], [[Resolution|resolution]] 3.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mzv]] is a 42 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=6MZV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MZV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mzv]] is a 42 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=6MZV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MZV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hoch_5816 ([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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6mzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzv OCA], [http://pdbe.org/6mzv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mzv RCSB], [http://www.ebi.ac.uk/pdbsum/6mzv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzv ProSAT]</span></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=6mzv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzv OCA], [https://pdbe.org/6mzv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mzv RCSB], [https://www.ebi.ac.uk/pdbsum/6mzv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/BMCT2_HALO1 BMCT2_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. One of 2 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 the stacked BMC-T trimers protruding to the exterior (PubMed:28642439, PubMed:30833088). The stacked trimers may serve as conduits to allow chemical flux across the protein shell, gated by Arg-70 which contacts Glu-69 in an adjacent subunit; they are flexible enough to play a role in accommodating variations in shell assembly (Probable).<ref>PMID:28642439</ref> <ref>PMID:30833088</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®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 6mzv" style="background-color:#fffaf0;"></div> | + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </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]]
| + | |
| Structural highlights
Function
BMCT2_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. One of 2 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 the stacked BMC-T trimers protruding to the exterior (PubMed:28642439, PubMed:30833088). The stacked trimers may serve as conduits to allow chemical flux across the protein shell, gated by Arg-70 which contacts Glu-69 in an adjacent subunit; they are flexible enough to play a role in accommodating variations in shell assembly (Probable).[1] [2] [3]
References
- ↑ Sutter M, Greber B, Aussignargues C, Kerfeld CA. Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell. Science. 2017 Jun 23;356(6344):1293-1297. doi: 10.1126/science.aan3289. PMID:28642439 doi:http://dx.doi.org/10.1126/science.aan3289
- ↑ Greber BJ, Sutter M, Kerfeld CA. The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. Structure. 2019 Feb 12. pii: S0969-2126(19)30017-6. doi:, 10.1016/j.str.2019.01.017. PMID:30833088 doi:http://dx.doi.org/10.1016/j.str.2019.01.017
- ↑ Greber BJ, Sutter M, Kerfeld CA. The Plasticity of Molecular Interactions Governs Bacterial Microcompartment Shell Assembly. Structure. 2019 Feb 12. pii: S0969-2126(19)30017-6. doi:, 10.1016/j.str.2019.01.017. PMID:30833088 doi:http://dx.doi.org/10.1016/j.str.2019.01.017
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