6guo
From Proteopedia
(Difference between revisions)
| (2 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Siderophore hydrolase EstA from Aspergillus nidulans== | |
| + | <StructureSection load='6guo' size='340' side='right'caption='[[6guo]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6guo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GUO FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=6guo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6guo OCA], [https://pdbe.org/6guo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6guo RCSB], [https://www.ebi.ac.uk/pdbsum/6guo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6guo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q5AV79_EMENI Q5AV79_EMENI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fungi utilize high-affinity chelators termed siderophores with chemically diverse structures to scavenge the essential nutrient iron from their surroundings. As they are among the strongest known Fe3+ binding agents, intracellular release of the heavy metal atom is facilitated by the activity of specific hydrolases. In this work, we report the characterization and x-ray structures of four siderophore esterases, AfEstB and AfSidJ from Aspergillus fumigatus, as well as AnEstB and AnEstA from Aspergillus nidulans. Even though they all display the conserved alpha/beta-hydrolase fold, we found remarkable structural and enzymatic discrepancies in their adaption to both related and chemically diverse substrates. A complex structure of AfEstB and its substrate triacetylfusarinine C gives insights into an active enzyme, with a tetrahedral coordination between the catalytic serine and the scissile ester bond. | ||
| - | + | Iron scavenging in Aspergillus species: Structural and biochemical insights into fungal siderophore esterases.,Ecker F, Haas H, Groll M, Huber E Angew Chem Int Ed Engl. 2018 Aug 1. doi: 10.1002/anie.201807093. PMID:30070018<ref>PMID:30070018</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6guo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus nidulans]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ecker F]] | ||
| + | [[Category: Groll M]] | ||
| + | [[Category: Haas H]] | ||
| + | [[Category: Huber EM]] | ||
Current revision
Siderophore hydrolase EstA from Aspergillus nidulans
| |||||||||||
