6guo: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "6guo" [edit=sysop:move=sysop] |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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]] | |||
Latest revision as of 12:35, 9 May 2024
Siderophore hydrolase EstA from Aspergillus nidulans
| ||||||||||||