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6mzu
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the HO BMC shell: BMC-TD focused structure, closed state== | |
| + | <StructureSection load='6mzu' size='340' side='right'caption='[[6mzu]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6mzu]] is a 42 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MZU FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6n06|6n06]], [[6mzy|6mzy]], [[6mzx|6mzx]], [[6mzv|6mzv]], [[6n07|6n07]], [[6n0f|6n0f]], [[6n09|6n09]], [[6n0g|6n0g]]</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=6mzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mzu OCA], [http://pdbe.org/6mzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mzu RCSB], [http://www.ebi.ac.uk/pdbsum/6mzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mzu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6mzu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Greber, B J]] | ||
| + | [[Category: Kerfeld, C A]] | ||
[[Category: Sutter, M]] | [[Category: Sutter, M]] | ||
| - | [[Category: | + | [[Category: Bmc fold]] |
| - | [[Category: | + | [[Category: Compartmentalization]] |
| + | [[Category: Microcompartment]] | ||
| + | [[Category: Shell]] | ||
| + | [[Category: Structural protein]] | ||
Revision as of 12:09, 13 March 2019
Cryo-EM structure of the HO BMC shell: BMC-TD focused structure, closed state
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