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| | ==Structure of Haliangium ochraceum BMC-T HO-5816== | | ==Structure of Haliangium ochraceum BMC-T HO-5816== |
| - | <StructureSection load='5v75' size='340' side='right' caption='[[5v75]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5v75' size='340' side='right'caption='[[5v75]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5v75]] is a 6 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=5V75 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V75 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5v75]] is a 6 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=5V75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V75 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v76|5v76]], [[5v74|5v74]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</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])</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=5v75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v75 OCA], [https://pdbe.org/5v75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v75 RCSB], [https://www.ebi.ac.uk/pdbsum/5v75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v75 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=5v75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v75 OCA], [http://pdbe.org/5v75 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v75 RCSB], [http://www.ebi.ac.uk/pdbsum/5v75 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v75 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Halo1]] | + | [[Category: Haliangium ochraceum DSM 14365]] |
| - | [[Category: Aussignargues, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Kerfeld, C A]] | + | [[Category: Aussignargues C]] |
| - | [[Category: Sutter, M]] | + | [[Category: Kerfeld CA]] |
| - | [[Category: Bacterial microcompartment]] | + | [[Category: Sutter M]] |
| - | [[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]
Publication Abstract from PubMed
Many bacteria contain primitive organelles composed entirely of protein. These bacterial microcompartments share a common architecture of an enzymatic core encapsulated in a selectively permeable protein shell; prominent examples include the carboxysome for CO2 fixation and catabolic microcompartments found in many pathogenic microbes. The shell sequesters enzymatic reactions from the cytosol, analogous to the lipid-based membrane of eukaryotic organelles. Despite available structural information for single building blocks, the principles of shell assembly have remained elusive. We present the crystal structure of an intact shell from Haliangium ochraceum, revealing the basic principles of bacterial microcompartment shell construction. Given the conservation among shell proteins of all bacterial microcompartments, these principles apply to functionally diverse organelles and can inform the design and engineering of shells with new functionalities.
Assembly principles and structure of a 6.5-MDa bacterial microcompartment shell.,Sutter M, Greber B, Aussignargues C, Kerfeld CA Science. 2017 Jun 23;356(6344):1293-1297. doi: 10.1126/science.aan3289. PMID:28642439[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ 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
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