6dyn: Difference between revisions
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The | ==C-terminal condensation domain of Ebony in complex with Histamine== | ||
<StructureSection load='6dyn' size='340' side='right'caption='[[6dyn]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6dyn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DYN 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]] 2.102Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HSM:HISTAMINE'>HSM</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=6dyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dyn OCA], [https://pdbe.org/6dyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dyn RCSB], [https://www.ebi.ac.uk/pdbsum/6dyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dyn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/EBO_DROME EBO_DROME] Nonribosomal peptide synthase which is required for the regulation of histamine and dopamine levels in various tissues through their condensation with beta-alanine (PubMed:12900414, PubMed:19715698, PubMed:25229196, PubMed:30705105). In epithelial glial cells, plays an essential role in the inactivation of histamine, the main neurotransmitter in the optical nerve system, by catalyzing the conversion of histamine into carcinine (PubMed:5782111, PubMed:12486147, PubMed:12900414, PubMed:25229196, PubMed:30705105). In the cuticle, catalyzes the condensation of beta-alanine with dopamine to form beta-alanyl-dopamine (NBAD), a metabolite involved in the pigmentation and sclerotization of the insect cuticle (PubMed:8580497, PubMed:11934851). Also, regulates the cuticular hydrocarbon composition in females (PubMed:31118901). Acts downstream of the body clock to regulate circadian behavioral rhythms (PubMed:17678856). Can also condense beta-alanine with biogenic amines tyramine, octopamine, and serotonin in vitro (PubMed:12900414, PubMed:19715698).<ref>PMID:11934851</ref> <ref>PMID:12486147</ref> <ref>PMID:12900414</ref> <ref>PMID:17678856</ref> <ref>PMID:19715698</ref> <ref>PMID:25229196</ref> <ref>PMID:30705105</ref> <ref>PMID:31118901</ref> <ref>PMID:5782111</ref> <ref>PMID:8580497</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The protein Ebony from Drosophila melanogaster plays a central role in the regulation of histamine and dopamine in various tissues through condensation of these amines with beta-alanine. Ebony is a rare example of a nonribosomal peptide synthetase (NRPS) from a higher eukaryote and contains a C-terminal sequence that does not correspond to any previously characterized NRPS domain. We have structurally characterized this C-terminal domain and have discovered that it adopts the aryl-alkylamine-N-acetyl transferase (AANAT) fold, which is unprecedented in NRPS biology. Through analysis of ligand-bound structures, activity assays, and binding measurements, we have determined how this atypical condensation domain is able to provide selectivity for both the carrier protein-bound amino acid and the amine substrates, a situation that remains unclear for standard condensation domains identified to date from NRPS assembly lines. These results demonstrate that the C terminus of Ebony encodes a eukaryotic example of an alternative type of NRPS condensation domain; they also illustrate how the catalytic components of such assembly lines are significantly more diverse than a minimal set of conserved functional domains. | |||
Drosophila melanogaster nonribosomal peptide synthetase Ebony encodes an atypical condensation domain.,Izore T, Tailhades J, Hansen MH, Kaczmarski JA, Jackson CJ, Cryle MJ Proc Natl Acad Sci U S A. 2019 Jan 31. pii: 1811194116. doi:, 10.1073/pnas.1811194116. PMID:30705105<ref>PMID:30705105</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6dyn" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Kaczmarski | </StructureSection> | ||
[[Category: Tailhades | [[Category: Drosophila melanogaster]] | ||
[[Category: Large Structures]] | |||
[[Category: Cryle MJ]] | |||
[[Category: Hansen MH]] | |||
[[Category: Izore T]] | |||
[[Category: Jackson CJ]] | |||
[[Category: Kaczmarski JA]] | |||
[[Category: Tailhades J]] | |||