5l22: Difference between revisions

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'''Unreleased structure'''


The entry 5l22 is ON HOLD  until Paper Publication
==PrtD T1SS ABC transporter==
<StructureSection load='5l22' size='340' side='right' caption='[[5l22]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5l22]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L22 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5l22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l22 OCA], [http://pdbe.org/5l22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l22 RCSB], [http://www.ebi.ac.uk/pdbsum/5l22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l22 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type-1 secretion systems (T1SSs) represent a widespread mode of protein secretion across the cell envelope in Gram-negative bacteria. The T1SS is composed of an inner-membrane ABC transporter, a periplasmic membrane-fusion protein, and an outer-membrane porin. These three components assemble into a complex spanning both membranes and providing a conduit for the translocation of unfolded polypeptides. We show that ATP hydrolysis and assembly of the entire T1SS complex is necessary for protein secretion. Furthermore, we present a 3.15-A crystal structure of AaPrtD, the ABC transporter found in the Aquifex aeolicus T1SS. The structure suggests a substrate entry window just above the transporter's nucleotide binding domains. In addition, highly kinked transmembrane helices, which frame a narrow channel not observed in canonical peptide transporters, are likely involved in substrate translocation. Overall, the AaPrtD structure supports a polypeptide transport mechanism distinct from alternating access.


Authors: Morgan, J.L.W., Zimmer, J.
Structure of a Type-1 Secretion System ABC Transporter.,Morgan JL, Acheson JF, Zimmer J Structure. 2017 Mar 7;25(3):522-529. doi: 10.1016/j.str.2017.01.010. Epub 2017, Feb 16. PMID:28216041<ref>PMID:28216041</ref>


Description: PrtD T1SS ABC transporter
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5l22" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Morgan, J L.W]]
[[Category: Zimmer, J]]
[[Category: Zimmer, J]]
[[Category: Morgan, J.L.W]]
[[Category: Abc transporter]]
[[Category: Atpase]]
[[Category: Protein transport]]
[[Category: Secretion]]
[[Category: T1ss]]
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