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==Native and K252c bound RebC-10x==
==Native and K252c bound RebC-10x==
<StructureSection load='4eip' size='340' side='right' caption='[[4eip]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
<StructureSection load='4eip' size='340' side='right'caption='[[4eip]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eip]] is a 2 chain structure with 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=4EIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EIP FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eip]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentzea_aerocolonigenes Lentzea aerocolonigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EIP FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.332&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r0c|2r0c]], [[2r0p|2r0p]], [[4eiq|4eiq]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rbmD, rebC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68170 Lechevalieria aerocolonigenes])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4eip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eip OCA], [https://pdbe.org/4eip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eip RCSB], [https://www.ebi.ac.uk/pdbsum/4eip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eip ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4eip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4eip RCSB], [http://www.ebi.ac.uk/pdbsum/4eip PDBsum]</span></td></tr>
</table>
<table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/Q8KI25_LENAE Q8KI25_LENAE]
== Publication Abstract from PubMed ==
The indolocarbazole biosynthetic enzymes StaC, InkE, RebC, and AtmC mediate the degree of oxidation of chromopyrrolic acid on route to the natural products staurosporine, K252a, rebeccamycin, and AT2433-A1, respectively. Here, we show that StaC and InkE, which mediate a net 4-electron oxidation, bind FAD with a micromolar K(d), whereas RebC and AtmC, which mediate a net 8-electron oxidation, bind FAD with a nanomolar K(d) while displaying the same FAD redox properties. We further create RebC-10x, a RebC protein with ten StaC-like amino acid substitutions outside of previously characterized FAD-binding motifs and the complementary StaC-10x. We find that these mutations mediate both FAD affinity and product specificity, with RebC-10x displaying higher StaC activity than StaC itself. X-ray structures of this StaC catalyst identify the substrate of StaC as 7-carboxy-K252c and suggest a unique mechanism for this FAD-dependent enzyme.
 
An Unusual Role for a Mobile Flavin in StaC-like Indolocarbazole Biosynthetic Enzymes.,Goldman PJ, Ryan KS, Hamill MJ, Howard-Jones AR, Walsh CT, Elliott SJ, Drennan CL Chem Biol. 2012 Jul 27;19(7):855-65. PMID:22840773<ref>PMID:22840773</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lechevalieria aerocolonigenes]]
[[Category: Large Structures]]
[[Category: Drennan, C L.]]
[[Category: Lentzea aerocolonigenes]]
[[Category: Elliott, S J.]]
[[Category: Drennan CL]]
[[Category: Goldman, P J.]]
[[Category: Elliott SJ]]
[[Category: Hamill, M J.]]
[[Category: Goldman PJ]]
[[Category: Howard-Jones, A R.]]
[[Category: Hamill MJ]]
[[Category: Ryan, K S.]]
[[Category: Howard-Jones AR]]
[[Category: Walsh, C T.]]
[[Category: Ryan KS]]
[[Category: Flavin adenine dinucleotide]]
[[Category: Walsh CT]]
[[Category: Indolocarbazole]]
[[Category: K252c]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]

Latest revision as of 11:04, 1 March 2024

Native and K252c bound RebC-10x

4eip, resolution 2.33Å

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