View source for 6nlu


==Circularly permuted Haliangium ochraceum BMC-H==
<StructureSection load='6nlu' size='340' side='right'caption='[[6nlu]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6nlu]] is a 2 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=6NLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NLU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.607&#8491;</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=6nlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nlu OCA], [https://pdbe.org/6nlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nlu RCSB], [https://www.ebi.ac.uk/pdbsum/6nlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nlu ProSAT]</span></td></tr>
</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;">
== Publication Abstract from PubMed ==
Microbes often augment their metabolism by conditionally constructing proteinaceous organelles, known as bacterial microcompartments (BMCs), that encapsulate enzymes to degrade organic compounds or assimilate CO2. BMCs self-assemble and are spatially delimited by a semi-permeable shell made up of hexameric, trimeric, and pentameric shell proteins. Bioengineers aim to recapitulate the organization and efficiency of these complex biological architectures by redesigning the shell to incorporate non-native enzymes from biotechnologically relevant pathways. To meet this challenge, a diverse set of synthetic biology tools are required, including methods to manipulate the properties of the shell as well as target and organize cargo encapsulation. We designed and determined the crystal structure of a synthetic shell protein building block with an inverted sidedness of its N- and C-terminal residues relative to its natural counterpart; the inversion targets genetically fused protein cargo to the lumen of the shell. Moreover, the titer of fluorescent protein cargo encapsulated using this strategy is controllable using an inducible tetracycline promoter. These results expand the available set of building blocks for precision engineering of BMC-based nanoreactors and are compatible with orthogonal methods which will facilitate the installation and organization of multi-enzyme pathways.

A designed bacterial microcompartment shell with tunable composition and precision cargo loading.,Ferlez B, Sutter M, Kerfeld CA Metab Eng. 2019 May 7;54:286-291. doi: 10.1016/j.ymben.2019.04.011. PMID:31075444<ref>PMID:31075444</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6nlu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Haliangium ochraceum]]
[[Category: Large Structures]]
[[Category: Ferlez B]]
[[Category: Kerfeld CA]]
[[Category: Sutter M]]