6n0g: Difference between revisions

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 <SX load='6n0g' size='340' side='right' viewer='molstar' caption='[[6n0g]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6n0g]] is a 57 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=6N0G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6N0G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6n0g]] is a 57 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=6N0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N0G FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6mzx|6mzx]], [[6mzy|6mzy]], [[6n06|6n06]], [[6mzu|6mzu]], [[6mzv|6mzv]], [[6n07|6n07]], [[6n0f|6n0f]], [[6n09|6n09]]</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]] 3.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hoch_5812 ([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]), 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=6n0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n0g OCA], [https://pdbe.org/6n0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n0g RCSB], [https://www.ebi.ac.uk/pdbsum/6n0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n0g ProSAT]</span></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=6n0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n0g OCA], [http://pdbe.org/6n0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n0g RCSB], [http://www.ebi.ac.uk/pdbsum/6n0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n0g ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/BMCT1_HALO1 BMCT1_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. This protein does not form 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 BMC-T trimers protruding to the exterior.<ref>PMID:28642439</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6n0g" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </SX>
-[[Category: Halo1]]
+[[Category: Haliangium ochraceum DSM 14365]]
 [[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]]