7ptt
From Proteopedia
(Difference between revisions)
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==In-situ structure of hexameric S-layer protein== | ==In-situ structure of hexameric S-layer protein== | ||
| - | <StructureSection load='7ptt' size='340' side='right'caption='[[7ptt]]' scene=''> | + | <StructureSection load='7ptt' size='340' side='right'caption='[[7ptt]], [[Resolution|resolution]] 7.97Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PTT FirstGlance]. <br> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PTT FirstGlance]. <br> | ||
| - | </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=7ptt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ptt OCA], [https://pdbe.org/7ptt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ptt RCSB], [https://www.ebi.ac.uk/pdbsum/7ptt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ptt ProSAT]</span></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]] 7.968Å</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=7ptt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ptt OCA], [https://pdbe.org/7ptt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ptt RCSB], [https://www.ebi.ac.uk/pdbsum/7ptt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ptt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Many prokaryotic cells are covered by an ordered, proteinaceous, sheet-like structure called a surface layer (S-layer). S-layer proteins (SLPs) are usually the highest copy number macromolecules in prokaryotes, playing critical roles in cellular physiology such as blocking predators, scaffolding membranes, and facilitating environmental interactions. Using electron cryomicroscopy of two-dimensional sheets, we report the atomic structure of the S-layer from the archaeal model organism Haloferax volcanii. This S-layer consists of a hexagonal array of tightly interacting immunoglobulin-like domains, which are also found in SLPs across several classes of archaea. Cellular tomography reveal that the S-layer is nearly continuous on the cell surface, completed by pentameric defects in the hexagonal lattice. We further report the atomic structure of the SLP pentamer, which shows markedly different relative arrangements of SLP domains needed to complete the S-layer. Our structural data provide a framework for understanding cell surfaces of archaea at the atomic level. | ||
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| + | Complete atomic structure of a native archaeal cell surface.,von Kugelgen A, Alva V, Bharat TAM Cell Rep. 2021 Nov 23;37(8):110052. doi: 10.1016/j.celrep.2021.110052. PMID:34818541<ref>PMID:34818541</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ptt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
In-situ structure of hexameric S-layer protein
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