2r0p

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[[Image:2r0p.jpg|left|200px]]
[[Image:2r0p.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2r0p |SIZE=350|CAPTION= <scene name='initialview01'>2r0p</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_2r0p", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=K2C:6,7,12,13-TETRAHYDRO-5H-INDOLO[2,3-A]PYRROLO[3,4-C]CARBAZOL-5-ONE'>K2C</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= rbmD, rebC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68170 Lechevalieria aerocolonigenes])
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-->
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|DOMAIN=
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{{STRUCTURE_2r0p| PDB=2r0p | SCENE= }}
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|RELATEDENTRY=[[2r0c|2R0C]], [[2r0g|2R0G]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r0p OCA], [http://www.ebi.ac.uk/pdbsum/2r0p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2r0p RCSB]</span>
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}}
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'''K252c-soaked RebC'''
'''K252c-soaked RebC'''
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[[Category: Drennan, C L.]]
[[Category: Drennan, C L.]]
[[Category: Ryan, K S.]]
[[Category: Ryan, K S.]]
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[[Category: flavin adenine dinucleotide]]
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[[Category: Flavin adenine dinucleotide]]
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[[Category: k252c]]
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[[Category: K252c]]
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[[Category: monooxygenase]]
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[[Category: Monooxygenase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:02:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:55:26 2008''
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Revision as of 13:02, 4 May 2008

Template:STRUCTURE 2r0p

K252c-soaked 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

2R0P 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 16:02:19 2008

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