6h3i

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m (Protected "6h3i" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6h3i is ON HOLD
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==Structural snapshots of the Type 9 protein translocon==
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<SX load='6h3i' size='340' side='right' viewer='molstar' caption='[[6h3i]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6h3i]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavobacterium_johnsoniae Flavobacterium johnsoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H3I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6H3I FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6h3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h3i OCA], [http://pdbe.org/6h3i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h3i RCSB], [http://www.ebi.ac.uk/pdbsum/6h3i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h3i ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The type 9 secretion system (T9SS) is the protein export pathway of bacteria of the Gram-negative Fibrobacteres-Chlorobi-Bacteroidetes superphylum and is an essential determinant of pathogenicity in severe periodontal disease. The central element of the T9SS is a so-far uncharacterized protein-conducting translocon located in the bacterial outer membrane. Here, using cryo-electron microscopy, we provide structural evidence that the translocon is the T9SS protein SprA. SprA forms an extremely large (36-strand) single polypeptide transmembrane beta-barrel. The barrel pore is capped on the extracellular end, but has a lateral opening to the external membrane surface. Structures of SprA bound to different components of the T9SS show that partner proteins control access to the lateral opening and to the periplasmic end of the pore. Our results identify a protein transporter with a distinctive architecture that uses an alternating access mechanism in which the two ends of the protein-conducting channel are open at different times.
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Authors: Deme, J.C., Lea, S.M.
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Type 9 secretion system structures reveal a new protein transport mechanism.,Lauber F, Deme JC, Lea SM, Berks BC Nature. 2018 Dec;564(7734):77-82. doi: 10.1038/s41586-018-0693-y. Epub 2018 Nov, 7. PMID:30405243<ref>PMID:30405243</ref>
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Description: Structural snapshots of the Type 9 protein translocon
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Deme, J.C]]
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<div class="pdbe-citations 6h3i" style="background-color:#fffaf0;"></div>
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[[Category: Lea, S.M]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Flavobacterium johnsoniae]]
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[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Deme, J C]]
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[[Category: Lea, S M]]
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[[Category: Protein transport]]
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[[Category: Type 9 secretion system type ix secretion system t9s folded protein secretion outer membrane protein]]

Current revision

Structural snapshots of the Type 9 protein translocon

6h3i, resolution 3.50Å

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