View source for 4pwv


==Structure of P450sky (CYP163B3), a cytochrome P450 from skyllamycin biosynthesis in complex with a peptidyl carrier protein domain==
<StructureSection load='4pwv' size='340' side='right'caption='[[4pwv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4pwv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._Acta_2897 Streptomyces sp. Acta 2897]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PWV 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=KH4:S-[2-({N-[(2R)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]+1H-IMIDAZOLE-4-CARBOTHIOATE'>KH4</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4pwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pwv OCA], [https://pdbe.org/4pwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pwv RCSB], [https://www.ebi.ac.uk/pdbsum/4pwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pwv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F2YRY7_9ACTN F2YRY7_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Studying the interplay between nonribosomal peptide synthetases (NRPS), a major source of secondary metabolites, and crucial external modifying enzymes is a challenging task since the interactions involved are often transient in nature. By applying a range of synthetic inhibitor-type compounds, a stabilized complex appropriate for structural analysis was generated for such a tailoring enzyme and an NRPS domain. The complex studied comprises an NRPS peptidyl carrier protein (PCP) domain bound to the Cytochrome P450 enzyme that is crucial for the provision of beta-hydroxylated amino acid precursors in the biosynthesis of the cyclic depsipeptide skyllamycin. The structure reveals that complex formation is governed by hydrophobic interactions, the presence of which can be controlled through minor alterations in PCP structure that enable selectivity amongst multiple highly similar PCP domains.

The structure of a transient complex of a nonribosomal Peptide synthetase and a cytochrome p450 monooxygenase.,Haslinger K, Brieke C, Uhlmann S, Sieverling L, Sussmuth RD, Cryle MJ Angew Chem Int Ed Engl. 2014 Aug 4;53(32):8518-22. doi: 10.1002/anie.201404977., Epub 2014 Jul 9. PMID:25044735<ref>PMID:25044735</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4pwv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. Acta 2897]]
[[Category: Cryle MJ]]
[[Category: Haslinger K]]