View source for 4iit


==The Phenylacetyl-CoA monooxygenase PaaABC subcomplex with phenylacetyl-CoA==
<StructureSection load='4iit' size='340' side='right'caption='[[4iit]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4iit]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_subsp._pneumoniae_MGH_78578 Klebsiella pneumoniae subsp. pneumoniae MGH 78578]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IIT 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]] 4.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAQ:PHENYLACETYL+COENZYME+A'>FAQ</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=4iit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iit OCA], [https://pdbe.org/4iit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iit RCSB], [https://www.ebi.ac.uk/pdbsum/4iit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iit ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A6T8I0_KLEP7 A6T8I0_KLEP7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phenylacetate degradation pathway is present in a wide range of microbes. A key component of this pathway is the four-subunit phenylacetyl-coenzyme A monooxygenase complex (PA-CoA MO, PaaACBE) that catalyzes the insertion of an oxygen in the aromatic ring of PA. This multicomponent enzyme represents a new family of monooxygenases. We have previously determined the structure of the PaaAC subcomplex of catalytic (A) and structural (C) subunits and shown that PaaACB form a stable complex. The PaaB subunit is unrelated to the small subunits of homologous monooxygenases and its role and organization of the PaaACB complex is unknown. From low-resolution crystal structure, electron microscopy and small angle X-ray scattering we show that the PaaACB complex forms heterohexamers, with a homodimer of PaaB bridging two PaaAC heterodimers. Modeling the interactions of reductase subunit PaaE with PaaACB suggested that a unique and conserved 'lysine bridge' constellation near the Fe-binding site in the PaaA subunit (Lys68, Glu49, Glu72 and Asp126) may form part of the electron transfer path from PaaE to the iron center. The crystal structure of the PaaA(K68Q/E49Q)-PaaC is very similar to the wild-type enzyme structure, but when combined with the PaaE subunit the mutant showed 20-50 times reduced activity, supporting the functional importance of the 'lysine bridge'.

Family of phenylacetyl-CoA monooxygenases differs in subunit organization from other monooxygenases.,Grishin AM, Ajamian E, Tao L, Bostina M, Zhang L, Trempe JF, Menard R, Rouiller I, Cygler M J Struct Biol. 2013 Sep 20. pii: S1047-8477(13)00242-6. doi:, 10.1016/j.jsb.2013.09.012. PMID:24055609<ref>PMID:24055609</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4iit" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae subsp. pneumoniae MGH 78578]]
[[Category: Large Structures]]
[[Category: Cygler M]]
[[Category: Grishin AM]]