View source for 8hnz


==Crystal structure of cytochrome P450 NasF5053 mutant E73S complexed with 6FCWP==
<StructureSection load='8hnz' size='340' side='right'caption='[[8hnz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hnz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._NRRL_F-5053 Streptomyces sp. NRRL F-5053]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HNZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HNZ FirstGlance]. <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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3I5:(3~{S},8~{a}~{S})-3-[(5-fluoranyl-1~{H}-indol-3-yl)methyl]-2,3,6,7,8,8~{a}-hexahydropyrrolo[1,2-a]pyrazine-1,4-dione'>3I5</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=8hnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hnz OCA], [https://pdbe.org/8hnz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hnz RCSB], [https://www.ebi.ac.uk/pdbsum/8hnz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hnz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A8I3B027_9ACTN A0A8I3B027_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heterodimeric tryptophan-containing diketopiperazines (HTDKPs) are an important class of bioactive secondary metabolites. Biosynthesis offers a practical opportunity to access their bioactive structural diversity, however, it is restricted by the limited substrate scopes of the HTDKPs-forming P450 dimerases. Herein, by genome mining and investigation of the sequence-product relationships, we unveiled three important residues (F387, F388 and E73) in these P450s that are pivotal for selecting different diketopiperazine (DKP) substrates in the upper binding pocket. Engineering these residues in Nas(F5053) significantly expanded its substrate specificity and enabled the collective biosynthesis, including 12 self-dimerized and at least 81 cross-dimerized HTDKPs. Structural and molecular dynamics analysis of F387G and E73S revealed that they control the substrate specificity via reducing steric hindrance and regulating substrate tunnels, respectively.

Engineering the Substrate Specificity of a P450 Dimerase Enables the Collective Biosynthesis of Heterodimeric Tryptophan-Containing Diketopiperazines.,Sun C, Ma BD, Li G, Tian W, Yang L, Peng H, Lin Z, Deng Z, Kong XD, Qu X Angew Chem Int Ed Engl. 2023 Jun 19;62(25):e202304994. doi: , 10.1002/anie.202304994. Epub 2023 May 8. PMID:37083030<ref>PMID:37083030</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hnz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. NRRL F-5053]]
[[Category: Kong XD]]
[[Category: Ma BD]]
[[Category: Qu X]]
[[Category: Tian W]]