3pcd
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 3PCD is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]] with CO3, FE and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 3PCD is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]] with CO3, FE and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3]]. Structure known Active Sites: ACA, ACB, ACC, ACD, ACE, ACF, VEA, VEB, VEC, VED, VEE and VEF. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3PCD OCA]]. |
==Reference== | ==Reference== | ||
The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates., Frazee RW, Orville AM, Dolbeare KB, Yu H, Ohlendorf DH, Lipscomb JD, Biochemistry. 1998 Feb 24;37(8):2131-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9485360 9485360] | The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates., Frazee RW, Orville AM, Dolbeare KB, Yu H, Ohlendorf DH, Lipscomb JD, Biochemistry. 1998 Feb 24;37(8):2131-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9485360 9485360] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| + | [[Category: Protocatechuate 3,4-dioxygenase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Lipscomb, J.D.]] | [[Category: Lipscomb, J.D.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:21:14 2007'' |
Revision as of 08:16, 30 October 2007
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PROTOCATECHUATE 3,4-DIOXYGENASE Y447H MUTANT
Overview
The essential active site Fe3+ of protocatechuate 3,4-dioxygenase [3, 4-PCD, subunit structure (alphabetaFe3+)12] is bound by axial ligands, Tyr447 (147beta) and His462 (162beta), and equatorial ligands, Tyr408, (108beta), His460 (160beta), and a solvent OH- (Wat827). Recent X-ray, crystallographic studies have shown that Tyr447 is dissociated from the, Fe3+ in the anaerobic 3,4-PCD complex with protocatechuate (PCA) [Orville, A. M., Lipscomb, J. D., and Ohlendorf, D. H. (1997) Biochemistry 36, 10052-10066]. The importance of Tyr447 to catalysis is investigated here, by site-directed mutation of this residue to His (Y447H), the first such, mutation reported for an aromatic ring cleavage dioxygenase containing, Fe3+. The crystal structure of Y447H (2.1 A resolution, R-factor of 0.181), is ... [(full description)]
About this Structure
3PCD is a [Protein complex] structure of sequences from [Pseudomonas putida] with CO3, FE and BME as [ligands]. Active as [Protocatechuate 3,4-dioxygenase], with EC number [1.13.11.3]. Structure known Active Sites: ACA, ACB, ACC, ACD, ACE, ACF, VEA, VEB, VEC, VED, VEE and VEF. Full crystallographic information is available from [OCA].
Reference
The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates., Frazee RW, Orville AM, Dolbeare KB, Yu H, Ohlendorf DH, Lipscomb JD, Biochemistry. 1998 Feb 24;37(8):2131-44. PMID:9485360
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