4r33
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4r33]] 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=4R33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R33 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4r33]] 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=4R33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R33 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</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=4r33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r33 OCA], [https://pdbe.org/4r33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r33 RCSB], [https://www.ebi.ac.uk/pdbsum/4r33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r33 ProSAT]</span></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=4r33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r33 OCA], [https://pdbe.org/4r33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r33 RCSB], [https://www.ebi.ac.uk/pdbsum/4r33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r33 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/C6FX51_STRAS C6FX51_STRAS] | [https://www.uniprot.org/uniprot/C6FX51_STRAS C6FX51_STRAS] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Streptomyces actuosus tryptophan lyase (NosL) is a radical SAM enzyme which catalyzes the synthesis of 3-methyl-2-indolic acid, a precursor in the synthesis of the promising antibiotic nosiheptide. The reaction involves cleavage of the tryptophan CalphaCbeta bond and recombination of the amino-acid-derived -COOH fragment at the indole ring. Reported herein is the 1.8 A resolution crystal structure of NosL complexed with its substrate. Unexpectedly, only one of the tryptophan amino hydrogen atoms is optimally placed for H abstraction by the SAM-derived 5'-deoxyadenosyl radical. This orientation, in turn, rules out the previously proposed delocalized indole radical as the species which undergoes CalphaCbeta bond cleavage. Instead, stereochemical considerations indicate that the reactive intermediate is a (.) NH tryptophanyl radical. A structure-based amino acid sequence comparison of NosL with the tyrosine lyases ThiH and HydG strongly suggests that an equivalent (.) NH radical operates in the latter enzymes. | ||
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| - | Crystal Structure of Tryptophan Lyase (NosL): Evidence for Radical Formation at the Amino Group of Tryptophan.,Nicolet Y, Zeppieri L, Amara P, Fontecilla-Camps JC Angew Chem Int Ed Engl. 2014 Oct 27;53(44):11840-4. doi: 10.1002/anie.201407320. , Epub 2014 Sep 5. PMID:25196319<ref>PMID:25196319</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4r33" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
X-ray structure of the tryptophan lyase NosL with Tryptophan and S-adenosyl-L-homocysteine bound
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