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| | <StructureSection load='6ner' size='340' side='right'caption='[[6ner]], [[Resolution|resolution]] 3.59Å' scene=''> | | <StructureSection load='6ner' size='340' side='right'caption='[[6ner]], [[Resolution|resolution]] 3.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ner]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Aj_13395 Aj 13395]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NER FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ner]] is a 30 chain structure with sequence from [https://en.wikipedia.org/wiki/Haliangium_ochraceum Haliangium ochraceum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NER FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 3.59Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hoch_5815 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=80816 AJ 13395])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6ner FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ner OCA], [http://pdbe.org/6ner PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ner RCSB], [http://www.ebi.ac.uk/pdbsum/6ner PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ner 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=6ner FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ner OCA], [https://pdbe.org/6ner PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ner RCSB], [https://www.ebi.ac.uk/pdbsum/6ner PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ner ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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> |
| | <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: Aj 13395]] | + | [[Category: Haliangium ochraceum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aussignargues, C]] | + | [[Category: Aussignargues C]] |
| - | [[Category: Kerfeld, C A]] | + | [[Category: Kerfeld CA]] |
| - | [[Category: McGuire, S]] | + | [[Category: McGuire S]] |
| - | [[Category: Sutter, M]] | + | [[Category: Sutter M]] |
| - | [[Category: Bacterial microcompartment]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
Bacterial microcompartments are subcellular compartments found in many prokaryotes; they consist of a protein shell that encapsulates enzymes that perform a variety of functions. The shell protects the cell from potentially toxic intermediates and colocalizes enzymes for higher efficiency. Accordingly, it is of considerable interest for biotechnological applications. We have previously structurally characterized an intact 40 nm shell comprising three different types of proteins. One of those proteins, BMC-H, forms a cyclic hexamer; here we have engineered a synthetic protein that consists of a tandem duplication of BMC-H connected by a short linker. The synthetic protein forms cyclic trimers that self-assemble to form a smaller (25 nm) icosahedral shell with gaps at the pentamer positions. When coexpressed in vivo with the pentamer fused to an affinity tag we can purify complete icosahedral shells. This engineered shell protein constitutes a minimal shell system to study permeability; reducing symmetry from 6- to 3-fold will allow for finer control of the pore environment. We have determined a crystal structure of this shell to guide rational engineering of this microcompartment shell for biotechnological applications.
Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of Forming Icosahedral Shell Assemblies.,Sutter M, McGuire S, Ferlez B, Kerfeld CA ACS Synth Biol. 2019 Mar 27. doi: 10.1021/acssynbio.9b00011. PMID:30901520[3]
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
- ↑ Sutter M, McGuire S, Ferlez B, Kerfeld CA. Structural Characterization of a Synthetic Tandem-Domain Bacterial Microcompartment Shell Protein Capable of Forming Icosahedral Shell Assemblies. ACS Synth Biol. 2019 Mar 27. doi: 10.1021/acssynbio.9b00011. PMID:30901520 doi:http://dx.doi.org/10.1021/acssynbio.9b00011
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