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4nao

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{{STRUCTURE_4nao| PDB=4nao | SCENE= }}
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==Crystal structure of EasH==
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===Crystal structure of EasH===
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<StructureSection load='4nao' size='340' side='right' caption='[[4nao]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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{{ABSTRACT_PUBMED_24361048}}
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== Structural highlights ==
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<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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2opw|2opw]], [[2a1x|2a1x]]</td></tr>
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<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>
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<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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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[[4nao]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NAO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024361048</ref><references group="xtra"/><references/>
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</div>
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[[Category: Havemann, J.]]
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== References ==
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[[Category: Janke, R.]]
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<references/>
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[[Category: Keller, U.]]
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__TOC__
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[[Category: Loll, B.]]
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</StructureSection>
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[[Category: Vogel, D.]]
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[[Category: Clapu]]
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[[Category: Havemann, J]]
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[[Category: Janke, R]]
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[[Category: Keller, U]]
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[[Category: Loll, B]]
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[[Category: Vogel, D]]
[[Category: Fe binding]]
[[Category: Fe binding]]
[[Category: Jelly-roll fold]]
[[Category: Jelly-roll fold]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]

Revision as of 09:24, 5 January 2015

Crystal structure of EasH

4nao, resolution 1.65Å

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