View source for 5wpu


==Crystal structure HpiC1 Y101S==
<StructureSection load='5wpu' size='340' side='right'caption='[[5wpu]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wpu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fischerella_sp._ATCC_43239 Fischerella sp. ATCC 43239]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WPU 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]] 1.39&#8491;</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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=5wpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wpu OCA], [https://pdbe.org/5wpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wpu RCSB], [https://www.ebi.ac.uk/pdbsum/5wpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wpu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A076NBW8_9CYAN A0A076NBW8_9CYAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hapalindole alkaloids are a structurally diverse class of cyanobacterial natural products defined by their varied polycyclic ring systems and diverse biological activities. These complex metabolites are generated from a common biosynthetic intermediate by the Stig cyclases in three mechanistic steps: a rare Cope rearrangement, 6-exo-trig cyclization, and electrophilic aromatic substitution. Here we report the structure of HpiC1, a Stig cyclase that catalyzes the formation of 12-epi-hapalindole U in vitro. The 1.5-A structure revealed a dimeric assembly with two calcium ions per monomer and with the active sites located at the distal ends of the protein dimer. Mutational analysis and computational methods uncovered key residues for an acid-catalyzed [3,3]-sigmatropic rearrangement, as well as specific determinants that control the position of terminal electrophilic aromatic substitution, leading to a switch from hapalindole to fischerindole alkaloids.

Structural basis of the Cope rearrangement and cyclization in hapalindole biogenesis.,Newmister SA, Li S, Garcia-Borras M, Sanders JN, Yang S, Lowell AN, Yu F, Smith JL, Williams RM, Houk KN, Sherman DH Nat Chem Biol. 2018 Apr;14(4):345-351. doi: 10.1038/s41589-018-0003-x. Epub 2018 , Mar 12. PMID:29531360<ref>PMID:29531360</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5wpu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fischerella sp. ATCC 43239]]
[[Category: Large Structures]]
[[Category: Garcia-Borras M]]
[[Category: Houk KN]]
[[Category: Li S]]
[[Category: Lowell AN]]
[[Category: Newmister SA]]
[[Category: Sanders JN]]
[[Category: Sherman DH]]
[[Category: Smith JL]]
[[Category: Williams RM]]
[[Category: Yang S]]
[[Category: Yu F]]