2r0g
From Proteopedia
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| - | [[Image:2r0g.jpg|left|200px]] | + | [[Image:2r0g.jpg|left|200px]] |
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| - | '''Chromopyrrolic acid-soaked RebC with bound 7-carboxy-K252c''' | + | {{Structure |
| + | |PDB= 2r0g |SIZE=350|CAPTION= <scene name='initialview01'>2r0g</scene>, resolution 2.37Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=7CK:7-carboxy-5-hydroxy-12,13-dihydro-6H-indolo[2,3-a]pyrrolo[3,4-c]carbazole'>7CK</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= rbmD, rebC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68170 Lechevalieria aerocolonigenes]) | ||
| + | }} | ||
| + | |||
| + | '''Chromopyrrolic acid-soaked RebC with bound 7-carboxy-K252c''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2R0G is a [ | + | 2R0G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lechevalieria_aerocolonigenes Lechevalieria aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R0G OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17873060 17873060] |
[[Category: Lechevalieria aerocolonigenes]] | [[Category: Lechevalieria aerocolonigenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:31:25 2008'' |
Revision as of 16:31, 20 March 2008
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| , resolution 2.37Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | rbmD, rebC (Lechevalieria aerocolonigenes) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Chromopyrrolic acid-soaked RebC with bound 7-carboxy-K252c
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
2R0G 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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