2r0c: Difference between revisions

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[[Image:2r0c.gif|left|200px]]
[[Image:2r0c.gif|left|200px]]


{{Structure
<!--
|PDB= 2r0c |SIZE=350|CAPTION= <scene name='initialview01'>2r0c</scene>, resolution 1.80&Aring;
The line below this paragraph, containing "STRUCTURE_2r0c", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= rbmD, rebC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68170 Lechevalieria aerocolonigenes])
-->
|DOMAIN=
{{STRUCTURE_2r0c| PDB=2r0c  | SCENE= }}  
|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>
}}


'''Structure of the substrate-free form of the rebeccamycin biosynthetic enzyme REBC'''
'''Structure of the substrate-free form of the rebeccamycin biosynthetic enzyme REBC'''
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[[Category: Drennan, C L.]]
[[Category: Drennan, C L.]]
[[Category: Ryan, K S.]]
[[Category: Ryan, K S.]]
[[Category: flavin adenine dinucleotide]]
[[Category: Flavin adenine dinucleotide]]
[[Category: monooxygenase]]
[[Category: Monooxygenase]]
[[Category: oxidoreductase]]
[[Category: Oxidoreductase]]
 
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Revision as of 13:01, 4 May 2008

File:2r0c.gif

Template:STRUCTURE 2r0c

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 Page seeded by OCA on Sun May 4 16:01:01 2008

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