2r0c
From Proteopedia
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|PDB= 2r0c |SIZE=350|CAPTION= <scene name='initialview01'>2r0c</scene>, resolution 1.80Å | |PDB= 2r0c |SIZE=350|CAPTION= <scene name='initialview01'>2r0c</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= rbmD, rebC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68170 Lechevalieria aerocolonigenes]) | |GENE= rbmD, rebC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68170 Lechevalieria aerocolonigenes]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0c OCA], [http://www.ebi.ac.uk/pdbsum/2r0c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2r0c RCSB]</span> | ||
}} | }} | ||
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[[Category: Drennan, C L.]] | [[Category: Drennan, C L.]] | ||
[[Category: Ryan, K S.]] | [[Category: Ryan, K S.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: FAD]] | ||
[[Category: flavin adenine dinucleotide]] | [[Category: flavin adenine dinucleotide]] | ||
[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:55:12 2008'' |
Revision as of 01:55, 31 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | rbmD, rebC (Lechevalieria aerocolonigenes) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the substrate-free form of the rebeccamycin biosynthetic enzyme REBC
Overview
The biosynthesis of rebeccamycin, an antitumor compound, involves the remarkable eight-electron oxidation of chlorinated chromopyrrolic acid. Although one rebeccamycin biosynthetic enzyme is capable of generating low levels of the eight-electron oxidation product on its own, a second protein, RebC, is required to accelerate product formation and eliminate side reactions. However, the mode of action of RebC was largely unknown. Using crystallography, we have determined a likely function for RebC as a flavin hydroxylase, captured two snapshots of its dynamic catalytic cycle, and trapped a reactive molecule, a putative substrate, in its binding pocket. These studies strongly suggest that the role of RebC is to sequester a reactive intermediate produced by its partner protein and to react with it enzymatically, preventing its conversion to a suite of degradation products that includes, at low levels, the desired product.
About this Structure
2R0C is a Single protein structure of sequence from Lechevalieria aerocolonigenes. Full crystallographic information is available from OCA.
Reference
Crystallographic trapping in the rebeccamycin biosynthetic enzyme RebC., Ryan KS, Howard-Jones AR, Hamill MJ, Elliott SJ, Walsh CT, Drennan CL, Proc Natl Acad Sci U S A. 2007 Sep 25;104(39):15311-6. Epub 2007 Sep 14. PMID:17873060
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