2r0p

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|PDB= 2r0p |SIZE=350|CAPTION= <scene name='initialview01'>2r0p</scene>, resolution 2.1&Aring;
|PDB= 2r0p |SIZE=350|CAPTION= <scene name='initialview01'>2r0p</scene>, resolution 2.1&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <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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|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>
|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=
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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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[[Category: Drennan, C L.]]
[[Category: Drennan, C L.]]
[[Category: Ryan, K S.]]
[[Category: Ryan, K S.]]
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[[Category: CL]]
 
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[[Category: FAD]]
 
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[[Category: K2C]]
 
[[Category: flavin adenine dinucleotide]]
[[Category: flavin adenine dinucleotide]]
[[Category: k252c]]
[[Category: k252c]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:31:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:55:26 2008''

Revision as of 01:55, 31 March 2008


PDB ID 2r0p

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: , ,
Gene: rbmD, rebC (Lechevalieria aerocolonigenes)
Related: 2R0C, 2R0G


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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