View source for 6hto


==Tryptophan lyase 'empty state'==
<StructureSection load='6hto' size='340' side='right'caption='[[6hto]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hto]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_actuosus Streptomyces actuosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HTO 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=6hto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hto OCA], [https://pdbe.org/6hto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hto RCSB], [https://www.ebi.ac.uk/pdbsum/6hto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hto ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C6FX51_STRAS C6FX51_STRAS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The radical S-adenosyl-l-methionine tryptophan lyase uses radical-based chemistry to convert l-tryptophan into 3-methyl-2-indolic acid, a fragment in the biosynthesis of the thiopeptide antibiotic nosiheptide. This complex reaction involves several successive steps corresponding to (i) the activation by a specific hydrogen-atom abstraction, (ii) an unprecedented *CO2(-) radical migration, (iii) a cyanide fragment release, and (iv) the termination of the radical-based reaction. In vitro study of this reaction is made more difficult because the enzyme produces a significant amount of a shunt product instead of the natural product. Here, using a combination of X-ray crystallography, electron paramagnetic resonance spectroscopy, and quantum and hybrid quantum mechanical/molecular mechanical calculations, we have deciphered the fine mechanism of the key *CO2(-) radical migration, highlighting how the preorganized active site of the protein tightly controls this reaction.

Radical S-Adenosyl-l-methionine Tryptophan Lyase (NosL): How the Protein Controls the Carboxyl Radical *CO2(-) Migration.,Amara P, Mouesca JM, Bella M, Martin L, Saragaglia C, Gambarelli S, Nicolet Y J Am Chem Soc. 2018 Nov 16. doi: 10.1021/jacs.8b09142. PMID:30418774<ref>PMID:30418774</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hto" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces actuosus]]
[[Category: Amara P]]
[[Category: Bella M]]
[[Category: Gambarelli S]]
[[Category: Martin L]]
[[Category: Mouesca JM]]
[[Category: Nicolet Y]]
[[Category: Saragaglia C]]