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| | <StructureSection load='5l22' size='340' side='right'caption='[[5l22]], [[Resolution|resolution]] 3.15Å' scene=''> | | <StructureSection load='5l22' size='340' side='right'caption='[[5l22]], [[Resolution|resolution]] 3.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5l22]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aquae Aquae]. 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://proteopedia.org/fgij/fg.htm?mol=5L22 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5l22]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5L22 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">abcT5, aq_1097 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224324 AQUAE])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://proteopedia.org/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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5l22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l22 OCA], [https://pdbe.org/5l22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l22 RCSB], [https://www.ebi.ac.uk/pdbsum/5l22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l22 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O67184_AQUAE O67184_AQUAE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aquae]] | + | [[Category: Aquifex aeolicus VF5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Morgan, J L.W]] | + | [[Category: Morgan JLW]] |
| - | [[Category: Zimmer, J]] | + | [[Category: Zimmer J]] |
| - | [[Category: Abc transporter]]
| + | |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Secretion]]
| + | |
| - | [[Category: T1ss]]
| + | |
| Structural highlights
Function
O67184_AQUAE
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Morgan JL, Acheson JF, Zimmer J. Structure of a Type-1 Secretion System ABC Transporter. Structure. 2017 Mar 7;25(3):522-529. doi: 10.1016/j.str.2017.01.010. Epub 2017, Feb 16. PMID:28216041 doi:http://dx.doi.org/10.1016/j.str.2017.01.010
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