4ii4: Difference between revisions

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New page: '''Unreleased structure''' The entry 4ii4 is ON HOLD Authors: Cygler, M., Grishin, A.M., Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) Description: The Phenylacetyl...
 
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'''Unreleased structure'''


The entry 4ii4 is ON HOLD
==The Phenylacetyl-CoA monooxygenase - mutant PaaA E49Q K68Q - PaaC wild type subcomplex with benzoyl-CoA==
<StructureSection load='4ii4' size='340' side='right'caption='[[4ii4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ii4]] is a 3 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=4II4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4II4 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]] 2.799&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BYC:BENZOYL+COENZYME+A'>BYC</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=4ii4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ii4 OCA], [https://pdbe.org/4ii4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ii4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ii4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ii4 ProSAT]</span></td></tr>
</table>
== Function ==
[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>


Authors: Cygler, M., Grishin, A.M., Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)
==See Also==
 
*[[Epoxidase 3D structures|Epoxidase 3D structures]]
Description: The Phenylacetyl-CoA monooxygenase -mutant PaaA E49Q K68Q -PaaC wild type subcomplex with benzoyl-CoA
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli str. K-12 substr. MG1655]]
[[Category: Large Structures]]
[[Category: Cygler M]]
[[Category: Grishin AM]]

Latest revision as of 18:23, 20 September 2023

The Phenylacetyl-CoA monooxygenase - mutant PaaA E49Q K68Q - PaaC wild type subcomplex with benzoyl-CoAThe Phenylacetyl-CoA monooxygenase - mutant PaaA E49Q K68Q - PaaC wild type subcomplex with benzoyl-CoA

Structural highlights

4ii4 is a 3 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 2.799Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4]

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
  4. ↑ Grishin AM, Ajamian E, Tao L, Zhang L, Menard R, Cygler M. Structural and functional studies of the Escherichia coli phenylacetyl-coa monooxygenase complex. J Biol Chem. 2011 Jan 19. PMID:21247899 doi:10.1074/jbc.M110.194423

4ii4, resolution 2.80Å

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