View source for 6htm


==X-ray structure of the tryptophan lyase NosL in complex with bound tryptamin==
<StructureSection load='6htm' size='340' side='right'caption='[[6htm]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6htm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_actuosus"_pinnert_et_al. "streptomyces actuosus" pinnert et al.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HTM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</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>, <scene name='pdbligand=TSS:2-(1H-INDOL-3-YL)ETHANAMINE'>TSS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6htk|6htk]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nosL, nocL, DMT42_23170 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1885 "Streptomyces actuosus" Pinnert et al.])</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=6htm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6htm OCA], [http://pdbe.org/6htm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6htm RCSB], [http://www.ebi.ac.uk/pdbsum/6htm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6htm ProSAT]</span></td></tr>
</table>
<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 6htm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Streptomyces actuosus pinnert et al]]
[[Category: Large Structures]]
[[Category: Amara, P]]
[[Category: Bella, M]]
[[Category: Gambarelli, S]]
[[Category: Mouesca, J M]]
[[Category: Nicolet, Y]]
[[Category: Saragaglia, C]]
[[Category: Antibiotic]]
[[Category: Nosiheptide]]
[[Category: Radical sam]]
[[Category: Tryptophan lyase]]