3pwq: Difference between revisions

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<StructureSection load='3pwq' size='340' side='right'caption='[[3pwq]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='3pwq' size='340' side='right'caption='[[3pwq]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3pwq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_mg1655 Escherichia coli mg1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PWQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3pwq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PWQ FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pvr|3pvr]], [[3pvt|3pvt]], [[3pvy|3pvy]], [[3pw1|3pw1]], [[3pw8|3pw8]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1390, JW1385, paaC, ydbP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511145 Escherichia coli MG1655]), b1388, JW1383, paaA, ydbO ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511145 Escherichia coli MG1655])</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=3pwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pwq OCA], [https://pdbe.org/3pwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pwq RCSB], [https://www.ebi.ac.uk/pdbsum/3pwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pwq ProSAT]</span></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=3pwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pwq OCA], [https://pdbe.org/3pwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pwq RCSB], [https://www.ebi.ac.uk/pdbsum/3pwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pwq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PAAC_ECOLI PAAC_ECOLI]] Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit C may be essential for structural integrity of the alpha subunit.<ref>PMID:9748275</ref> <ref>PMID:16997993</ref> <ref>PMID:20660314</ref>  [[https://www.uniprot.org/uniprot/PAAA_ECOLI PAAA_ECOLI]] Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA.<ref>PMID:9748275</ref> <ref>PMID:16997993</ref> <ref>PMID:20660314</ref> <ref>PMID:21247899</ref> 
[https://www.uniprot.org/uniprot/PAAC_ECOLI PAAC_ECOLI] Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit C may be essential for structural integrity of the alpha subunit.<ref>PMID:9748275</ref> <ref>PMID:16997993</ref> <ref>PMID:20660314</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The utilization of phenylacetic acid (PA) in Escherichia coli occurs through a hybrid pathway that shows features of both aerobic and anaerobic metabolism. Oxygenation of the aromatic ring is performed by a multisubunit phenylacetyl-coenzyme A oxygenase complex that shares remote homology of two subunits to well-studied bacterial multicomponent mono-oxygenases (BMMs) and was postulated to form a new BMM subfamily. We expressed the subunits PaaA,B,C,D,E of the PA-CoA oxygenase and showed that PaaABC, PaaAC and PaaBC form stable sub-complexes that can be purified. In vitro reconstitution of the oxygenase subunits showed that each of the PaaA,B,C and E subunits are necessary for catalysis, while PaaD is not essential. We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. We conclude that PaaAC forms a catalytic core with a monooxygenase fold with PaaA being the catalytic alpha subunit and PaaC - the structural beta subunit. PaaAC forms hetero-tetramers that are organized very differently from other known multisubunit monooxygenases and lacks their conservative network of hydrogen bonds between the di-iron center and protein surface, suggesting different association with the reductase and different mechanism of electron transport. The PaaA structure shows adaptation of the common access route to the active site for binding a CoA-bound substrate. The enzyme-substrate complex shows the orientation of the aromatic ring, which is poised for oxygenation at the ortho-position, in accordance with the expected chemistry. The PA-CoA oxygenase complex serves as a paradigm for the new subfamily multicomponent monooxygenases comprising several hundreds of homologs.
 
Structural and functional studies of the Escherichia coli phenylacetyl-coa monooxygenase complex.,Grishin AM, Ajamian E, Tao L, Zhang L, Menard R, Cygler M J Biol Chem. 2011 Jan 19. PMID:21247899<ref>PMID:21247899</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3pwq" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli mg1655]]
[[Category: Escherichia coli str. K-12 substr. MG1655]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Cygler M]]
[[Category: Cygler, M]]
[[Category: Grishin AM]]
[[Category: Grishin, A M]]
[[Category: Bacterial multicomponent monooxygenase]]
[[Category: Bsgi]]
[[Category: Ferritin-like fold]]
[[Category: Oxidoreductase]]
[[Category: Protein-protein complex]]

Latest revision as of 16:34, 1 March 2024

The Phenylacetyl-CoA monooxygenase PaaAC subcomplexThe Phenylacetyl-CoA monooxygenase PaaAC subcomplex

Structural highlights

3pwq is a 12 chain structure with sequence from Escherichia coli str. K-12 substr. MG1655. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.65Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAAC_ECOLI Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit C may be essential for structural integrity of the alpha subunit.[1] [2] [3]

See Also

References

  1. ↑ Ferrandez A, Minambres B, Garcia B, Olivera ER, Luengo JM, Garcia JL, Diaz E. Catabolism of phenylacetic acid in Escherichia coli. Characterization of a new aerobic hybrid pathway. J Biol Chem. 1998 Oct 2;273(40):25974-86. PMID:9748275
  2. ↑ Fernandez C, Ferrandez A, Minambres B, Diaz E, Garcia JL. Genetic characterization of the phenylacetyl-coenzyme A oxygenase from the aerobic phenylacetic acid degradation pathway of Escherichia coli. Appl Environ Microbiol. 2006 Nov;72(11):7422-6. Epub 2006 Sep 22. PMID:16997993 doi:10.1128/AEM.01550-06
  3. ↑ Teufel R, Mascaraque V, Ismail W, Voss M, Perera J, Eisenreich W, Haehnel W, Fuchs G. Bacterial phenylalanine and phenylacetate catabolic pathway revealed. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14390-5. doi:, 10.1073/pnas.1005399107. Epub 2010 Jul 21. PMID:20660314 doi:10.1073/pnas.1005399107

3pwq, resolution 2.65Å

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