4nao: Difference between revisions
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==Crystal structure of EasH== | |||
=== | <StructureSection load='4nao' size='340' side='right' caption='[[4nao]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4nao]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clapu Clapu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NAO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NAO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2opw|2opw]], [[2a1x|2a1x]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">easH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5111 CLAPU])</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=4nao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nao OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nao RCSB], [http://www.ebi.ac.uk/pdbsum/4nao PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The tripeptide chains of the ergopeptines, a class of pharmacologically important D-lysergic acid alkaloid peptides, are arranged in a unique bicyclic cyclol based on an amino-terminal alpha-hydroxyamino acid and a terminal orthostructure. D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases LPS1 and LPS2 of the ergot fungus Claviceps purpurea and released as N-(D-lysergyl-aminoacyl)-lactams. We show total enzymatic synthesis of ergopeptines catalyzed by a Fe2+/2-ketoglutarate-dependent dioxygenase (EasH) in conjunction with LPS1/LPS2. Analysis of the reaction indicated that EasH introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group. Sequence analysis revealed that EasH belongs to the wide and diverse family of the phytanoyl coenzyme A hydroxylases. We provide a high-resolution crystal structure of EasH that is most similar to that of phytanoyl coenzyme A hydroxylase, PhyH, from human. | |||
Cyclolization of D-Lysergic Acid Alkaloid Peptides.,Havemann J, Vogel D, Loll B, Keller U Chem Biol. 2013 Dec 18. pii: S1074-5521(13)00417-1. doi:, 10.1016/j.chembiol.2013.11.008. PMID:24361048<ref>PMID:24361048</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Havemann, J | == References == | ||
[[Category: Janke, R | <references/> | ||
[[Category: Keller, U | __TOC__ | ||
[[Category: Loll, B | </StructureSection> | ||
[[Category: Vogel, D | [[Category: Clapu]] | ||
[[Category: Havemann, J]] | |||
[[Category: Janke, R]] | |||
[[Category: Keller, U]] | |||
[[Category: Loll, B]] | |||
[[Category: Vogel, D]] | |||
[[Category: Fe binding]] | [[Category: Fe binding]] | ||
[[Category: Jelly-roll fold]] | [[Category: Jelly-roll fold]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
