6v9z

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Current revision (14:36, 6 March 2024) (edit) (undo)
 
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<SX load='6v9z' size='340' side='right' viewer='molstar' caption='[[6v9z]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
<SX load='6v9z' size='340' side='right' viewer='molstar' caption='[[6v9z]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6v9z]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V9Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V9Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6v9z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V9Z FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cthe_0534 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203119 Clostridium thermocellum]), Cthe_0535 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203119 Clostridium thermocellum])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.35&#8491;</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=6v9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v9z OCA], [http://pdbe.org/6v9z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v9z RCSB], [http://www.ebi.ac.uk/pdbsum/6v9z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v9z ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6v9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v9z OCA], [https://pdbe.org/6v9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v9z RCSB], [https://www.ebi.ac.uk/pdbsum/6v9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v9z ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A3DCU1_ACET2 A3DCU1_ACET2]
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The peptidase-containing ATP-binding cassette transporters (PCATs) are unique members of the ABC transporter family that proteolytically process and export peptides and proteins. Each PCAT contains two peptidase domains that cleave off the secretion signal, two transmembrane domains forming a translocation pathway, and two nucleotide-binding domains that hydrolyze ATP. Previously the crystal structures of a PCAT from Clostridium thermocellum (PCAT1) were determined in the absence and presence of ATP, revealing how ATP binding regulates the protease activity and access to the translocation pathway. However, how the substrate CtA, a 90-residue polypeptide, is recognized by PCAT1 remained elusive. To address this question, we determined the structure of the PCAT1-CtA complex by electron cryo-microscopy (cryo-EM) to 3.4 A resolution. The structure shows that two CtAs are bound via their N-terminal leader peptides, but only one is positioned for cleavage and translocation. Based on these results, we propose a model of how substrate cleavage, ATP hydrolysis, and substrate translocation are coordinated in a transport cycle.
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Structural basis of substrate recognition by a polypeptide processing and secretion transporter.,Kieuvongngam V, Olinares PDB, Palillo A, Oldham ML, Chait BT, Chen J Elife. 2020 Jan 14;9. pii: 51492. doi: 10.7554/eLife.51492. PMID:31934861<ref>PMID:31934861</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6v9z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Clostridium thermocellum]]
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[[Category: Acetivibrio thermocellus ATCC 27405]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, J]]
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[[Category: Chen J]]
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[[Category: Kieuvongngam, V]]
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[[Category: Kieuvongngam V]]
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[[Category: Oldham, M L]]
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[[Category: Oldham ML]]
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[[Category: Atp-binding cassette]]
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[[Category: Protein transport]]
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Current revision

Cryo-EM structure of PCAT1 bound to its CtA peptide substrate

6v9z, resolution 3.35Å

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