6b05: Difference between revisions
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<StructureSection load='6b05' size='340' side='right' caption='[[6b05]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='6b05' size='340' side='right' caption='[[6b05]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6b05]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B05 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6b05]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath] and [http://en.wikipedia.org/wiki/Erwinia_carotovora_subsp._atroseptica Erwinia carotovora subsp. atroseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B05 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b03|6b03]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b03|6b03]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ECA0879 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=218491 Erwinia carotovora subsp. atroseptica]), FD2, PETF, PETF1, At1g60950, T7P1.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=6b05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b05 OCA], [http://pdbe.org/6b05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b05 RCSB], [http://www.ebi.ac.uk/pdbsum/6b05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b05 ProSAT]</span></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=6b05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b05 OCA], [http://pdbe.org/6b05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b05 RCSB], [http://www.ebi.ac.uk/pdbsum/6b05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b05 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FER2_ARATH FER2_ARATH]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | [[http://www.uniprot.org/uniprot/FER2_ARATH FER2_ARATH]] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Iron is essential for life. Accessing iron from the environment can be a limiting factor that determines success in a given environmental niche. For bacteria, access of chelated iron from the environment is often mediated by TonB-dependent transporters (TBDTs), which are beta-barrel proteins that form sophisticated channels in the outer membrane. Reports of iron-bearing proteins being used as a source of iron indicate specific protein import reactions across the bacterial outer membrane. The molecular mechanism by which a folded protein can be imported in this way had remained mysterious, as did the evolutionary process that could lead to such a protein import pathway. How does the bacterium evolve the specificity factors that would be required to select and import a protein encoded on another organism's genome? We describe here a model whereby the plant iron-bearing protein ferredoxin can be imported across the outer membrane of the plant pathogen Pectobacterium by means of a Brownian ratchet mechanism, thereby liberating iron into the bacterium to enable its growth in plant tissues. This import pathway is facilitated by FusC, a member of the same protein family as the mitochondrial processing peptidase (MPP). The Brownian ratchet depends on binding sites discovered in crystal structures of FusC that engage a linear segment of the plant protein ferredoxin. Sequence relationships suggest that the bacterial gene encoding FusC has previously unappreciated homologues in plants and that the protein import mechanism employed by the bacterium is an evolutionary echo of the protein import pathway in plant mitochondria and plastids. | |||
FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.,Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T PLoS Biol. 2018 Aug 2;16(8):e2006026. doi: 10.1371/journal.pbio.2006026., eCollection 2018 Aug. PMID:30071011<ref>PMID:30071011</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6b05" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | |||
[[Category: Erwinia carotovora subsp. atroseptica]] | |||
[[Category: Grinter, R]] | [[Category: Grinter, R]] | ||
[[Category: Ferredoxin binding]] | [[Category: Ferredoxin binding]] | ||