7qf6
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF== | |
| - | + | <StructureSection load='7qf6' size='340' side='right'caption='[[7qf6]], [[Resolution|resolution]] 1.87Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[7qf6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QF6 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7qf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qf6 OCA], [https://pdbe.org/7qf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qf6 RCSB], [https://www.ebi.ac.uk/pdbsum/7qf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qf6 ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: Poonsiri | + | == Function == |
| - | [[Category: | + | [https://www.uniprot.org/uniprot/SIDF_ASPFU SIDF_ASPFU] Hydroxyornithine transacylase; part of the siderophore biosynthetic pathway (PubMed:17845073, PubMed:23617799). Aspergillus fumigatus produces 4 types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of 3 N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).<ref>PMID:15504822</ref> <ref>PMID:16113265</ref> <ref>PMID:17845073</ref> <ref>PMID:21622789</ref> <ref>PMID:22106303</ref> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus fumigatus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Demitri N]] | ||
| + | [[Category: Poonsiri T]] | ||
| + | [[Category: Stefano B]] | ||
Revision as of 09:58, 14 December 2022
N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF
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