6g7n
From Proteopedia
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<StructureSection load='6g7n' size='340' side='right' caption='[[6g7n]], [[Resolution|resolution]] 1.10Å' scene=''> | <StructureSection load='6g7n' size='340' side='right' caption='[[6g7n]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6g7n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G7N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6g7n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Triei Triei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6G7N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6G7N FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tery_3377 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=203124 TRIEI])</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=6g7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g7n OCA], [http://pdbe.org/6g7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g7n RCSB], [http://www.ebi.ac.uk/pdbsum/6g7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g7n 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=6g7n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6g7n OCA], [http://pdbe.org/6g7n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6g7n RCSB], [http://www.ebi.ac.uk/pdbsum/6g7n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6g7n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Atmospheric nitrogen fixation by photosynthetic cyanobacteria (diazotrophs) strongly influences oceanic primary production and in turn affects global biogeochemical cycles. Species of the genus Trichodesmium are major contributors to marine diazotrophy, accounting for a significant proportion of the fixed nitrogen in tropical and subtropical oceans. However, Trichodesmium spp. are metabolically constrained by the availability of iron, an essential element for both the photosynthetic apparatus and the nitrogenase enzyme. Survival strategies in low-iron environments are typically poorly characterized at the molecular level, as these bacteria are recalcitrant to genetic manipulation. Here, we studied a homolog of the iron deficiency-induced A (IdiA)/ferric uptake transporter A (FutA) protein, Tery_3377, which has been used as an in situ iron-stress biomarker. IdiA/FutA has an ambiguous function in cyanobacteria, with its homologs hypothesized to be involved in distinct processes depending on their cellular localization. Using signal sequence fusions to GFP and heterologous expression in the model cyanobacterium Synechocystis sp. PCC 6803 we show that Tery_3377 is targeted to the periplasm by the twin-arginine translocase and can complement the deletion of the native Synechocystis ferric-iron ABC transporter periplasmic binding protein (FutA2). EPR spectroscopy revealed that purified recombinant Tery_3377 has specificity for iron in the Fe(3+) state, and an X-ray crystallography determined structure uncovered a functional iron substrate-binding domain, with Fe(3+) penta-coordinated by protein and buffer ligands. Our results support assignment of Tery_3377 as a functional FutA subunit of an Fe(3+) ABC-transporter, but do not rule out that it also has dual IdiA function. | ||
| + | |||
| + | Structural and functional characterisation of IdiA/FutA (Tery_3377), an iron binding protein from the ocean diazotroph Trichodesmium erythraeum.,Polyviou D, Machelett MM, Hitchcock A, Baylay AJ, MacMillan F, Moore CM, Bibby TS, Tews I J Biol Chem. 2018 Sep 14. pii: RA118.001929. doi: 10.1074/jbc.RA118.001929. PMID:30217820<ref>PMID:30217820</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6g7n" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Triei]] | ||
[[Category: Machelett, M M]] | [[Category: Machelett, M M]] | ||
[[Category: Tews, I]] | [[Category: Tews, I]] | ||
Revision as of 08:43, 26 September 2018
Trichodesmium Tery_3377 (IdiA) (FutA) with iron and alanine ligand.
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Categories: Triei | Machelett, M M | Tews, I | Abc-transporter | Futa | Idia | Iron | Metal binding protein
