6SLS

Flavin-dependent tryptophan 6-halogenase Thal in complex with FAD

Summary for 6SLS

• Entry DOI: 10.2210/pdb6sls/pdb
• Related: 6H43 6H44 6IB5 6SLT
• Descriptor: Tryptophan 6-halogenase, GLYCEROL, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: tryptophan halogenase, thdh, flavoprotein, thal, fad
• Biological source: Streptomyces albogriseolus
• Total number of polymer chains: 2
• Total formula weight: 122915.30

Authors

Moritzer, A.,Niemann, H.H. (deposition date: 2019-08-20, release date: 2019-10-16, Last modification date: 2024-01-24)

Primary citation

Moritzer, A.C.,Niemann, H.H.
Binding of FAD and tryptophan to the tryptophan 6-halogenase Thal is negatively coupled.
Protein Sci., 28:2112-2118, 2019

PubMed Abstract: Flavin-dependent halogenases require reduced flavin adenine dinucleotide (FADH ), O , and halide salts to halogenate their substrates. We describe the crystal structures of the tryptophan 6-halogenase Thal in complex with FAD or with both tryptophan and FAD. If tryptophan and FAD were soaked simultaneously, both ligands showed impaired binding and in some cases only the adenosine monophosphate or the adenosine moiety of FAD was resolved, suggesting that tryptophan binding increases the mobility mainly of the flavin mononucleotide moiety. This confirms a negative cooperativity between the binding of substrate and cofactor that was previously described for other tryptophan halogenases. Binding of substrate to tryptophan halogenases reduces the affinity for the oxidized cofactor FAD presumably to facilitate the regeneration of FADH by flavin reductases.

PubMed: 31589794
DOI: 10.1002/pro.3739

Experimental method

X-RAY DIFFRACTION (2.32 Å)