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| | ==The structure of the fused permuted hexameric shell protein MSM0275 from the RMM microcompartment== | | ==The structure of the fused permuted hexameric shell protein MSM0275 from the RMM microcompartment== |
| - | <StructureSection load='5l39' size='340' side='right' caption='[[5l39]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='5l39' size='340' side='right'caption='[[5l39]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l39]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L39 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L39 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l39]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L39 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5l37|5l37]], [[5l38|5l38]], [[5suh|5suh]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5l39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l39 OCA], [http://pdbe.org/5l39 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l39 RCSB], [http://www.ebi.ac.uk/pdbsum/5l39 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l39 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=5l39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l39 OCA], [https://pdbe.org/5l39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l39 RCSB], [https://www.ebi.ac.uk/pdbsum/5l39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l39 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0QP52_MYCS2 A0QP52_MYCS2] |
| | <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: Kimber, M S]] | + | [[Category: Large Structures]] |
| - | [[Category: Mallette, E]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Bacterial microcompartment]] | + | [[Category: Kimber MS]] |
| - | [[Category: Fused permuted hexameric shell protein]] | + | [[Category: Mallette E]] |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
A0QP52_MYCS2
Publication Abstract from PubMed
Bacterial microcompartments are bacterial analogs of eukaryotic organelles in that they spatially segregate aspects of cellular metabolism, but they do so by building not a lipid membrane but a thin polyhedral protein shell. Although multiple shell protein structures are known for several microcompartment types, additional uncharacterized components complicate systematic investigations of shell architecture. We report here the structures of all four proteins proposed to form the shell of an uncharacterized microcompartment designated the Rhodococcus and Mycobacterium microcompartment (RMM), which, along with crystal interactions and docking studies, suggests possible models for the particle's vertex and edge organization. MSM0272 is a typical hexameric beta-sandwich shell protein thought to form the bulk of the facet. MSM0273 is a pentameric beta-barrel shell protein that likely plugs the vertex of the particle. MSM0271 is an unusual double-ringed bacterial microcompartment shell protein whose rings are organized in an offset position relative to all known related proteins. MSM0275 is related to MSM0271 but self-organizes as linear strips that may line the facet edge; here, the presence of a novel extendable loop may help ameliorate poor packing geometry of the rigid main particle at the angled edges. In contrast to previously characterized homologs, both of these proteins show closed pores at both ends. This suggests a model where key interactions at the vertex and edges are mediated at the inner layer of the shell by MSM0271 (encircling MSM0273) and MSM0275, and the facet is built from MSM0272 hexamers tiling in the outer layer of the shell.
A Complete Structural Inventory of the Mycobacterial Microcompartment Shell Proteins Constrains Models of Global Architecture and Transport.,Mallette E, Kimber MS J Biol Chem. 2017 Jan 27;292(4):1197-1210. doi: 10.1074/jbc.M116.754093. Epub, 2016 Dec 6. PMID:27927988[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mallette E, Kimber MS. A Complete Structural Inventory of the Mycobacterial Microcompartment Shell Proteins Constrains Models of Global Architecture and Transport. J Biol Chem. 2017 Jan 27;292(4):1197-1210. doi: 10.1074/jbc.M116.754093. Epub, 2016 Dec 6. PMID:27927988 doi:http://dx.doi.org/10.1074/jbc.M116.754093
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