2oa1: Difference between revisions
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2oa1 ConSurf]. | ||
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== References == | == References == |
Revision as of 21:03, 8 February 2016
Crystal Structure of RebH, a FAD-dependent halogenase from Lechevalieria aerocolonigenes, the L-Tryptophan with FAD complexCrystal Structure of RebH, a FAD-dependent halogenase from Lechevalieria aerocolonigenes, the L-Tryptophan with FAD complex
Structural highlights
Function[REBH_NOCAE] Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. Catalyze the chlorination of tryptophan (Trp) at C7 position to yield 7-chlorotryptophan. The reaction between FADH2, Cl-, and O2 generates the powerful oxidant HOCl, which is presumed to carry out the chlorination reaction. The reaction of HOCl with the active site Lys-79 generates a lysine chloramine, which plays a key role in directing regiospecific chlorination of substrate in this important class of biosynthetic enzymes. It is also able to use bromide ions to generate monobrominated Trp.[1] [2] [3] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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