This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4nao

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structure of EasH==
==Crystal structure of EasH==
-
<StructureSection load='4nao' size='340' side='right' caption='[[4nao]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
+
<StructureSection load='4nao' size='340' side='right'caption='[[4nao]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== 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>
+
<table><tr><td colspan='2'>[[4nao]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Claviceps_purpurea Claviceps purpurea]. 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 [https://proteopedia.org/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>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nao OCA], [https://pdbe.org/4nao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nao RCSB], [https://www.ebi.ac.uk/pdbsum/4nao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nao ProSAT]</span></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://pdbe.org/4nao PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nao RCSB], [http://www.ebi.ac.uk/pdbsum/4nao PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nao ProSAT]</span></td></tr>
+
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/EASH_CLAP2 EASH_CLAP2] Dioxygenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which 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 (PubMed:24361048).[UniProtKB:Q50EL0]<ref>PMID:14700635</ref> <ref>PMID:14732265</ref> <ref>PMID:15904941</ref> <ref>PMID:16538694</ref> <ref>PMID:17560817</ref> <ref>PMID:19139103</ref> <ref>PMID:20118373</ref> <ref>PMID:20735127</ref> <ref>PMID:21409592</ref> <ref>PMID:21494745</ref> <ref>PMID:24361048</ref> <ref>PMID:17308187</ref> <ref>PMID:17720822</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 22: Line 22:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Clapu]]
+
[[Category: Claviceps purpurea]]
-
[[Category: Havemann, J]]
+
[[Category: Large Structures]]
-
[[Category: Janke, R]]
+
[[Category: Havemann J]]
-
[[Category: Keller, U]]
+
[[Category: Janke R]]
-
[[Category: Loll, B]]
+
[[Category: Keller U]]
-
[[Category: Vogel, D]]
+
[[Category: Loll B]]
-
[[Category: Fe binding]]
+
[[Category: Vogel D]]
-
[[Category: Jelly-roll fold]]
+
-
[[Category: Oxidoreductase]]
+

Revision as of 08:18, 11 January 2023

Crystal structure of EasH

PDB ID 4nao

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nao"
Personal tools