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3pck
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 3PCK 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 FE, BME and NNO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ | + | 3PCK 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 FE, BME and NNO 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=3PCK OCA]]. |
==Reference== | ==Reference== | ||
Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding., Orville AM, Lipscomb JD, Ohlendorf DH, Biochemistry. 1997 Aug 19;36(33):10052-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9254600 9254600] | Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding., Orville AM, Lipscomb JD, Ohlendorf DH, Biochemistry. 1997 Aug 19;36(33):10052-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9254600 9254600] | ||
[[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: transition-state analog complex]] | [[Category: transition-state analog complex]] | ||
| - | ''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 10:21:19 2007'' |
Revision as of 08:16, 30 October 2007
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STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 6-HYDROXYNICOTINIC ACID N-OXIDE
Overview
Protocatechuate 3,4-dioxygenase (3,4-PCD) utilizes a ferric ion to, catalyze the aromatic ring cleavage of 3,4-dihydroxybenzoate (PCA) by, incorporation of both atoms of dioxygen to yield beta-carboxy-cis, cis-muconate. The crystal structures of the anaerobic 3,4-PCD.PCA complex, aerobic complexes with two heterocyclic PCA analogs, 2-hydroxyisonicotinic, acid N-oxide (INO) and 6-hydroxynicotinic acid N-oxide (NNO), and ternary, complexes of 3,4-PCD.INO.CN and 3,4-PCD. NNO.CN have been determined at, 2.1-2.2 A resolution and refined to R-factors between 0.165 and 0.184., PCA, INO, and NNO form very similar, asymmetrically chelated complexes, with the active site Fe3+ that result in dissociation of the endogenous, axial tyrosinate Fe3+ ligand, Tyr447 (147beta). After its release from the, ... [(full description)]
About this Structure
3PCK is a [Protein complex] structure of sequences from [Pseudomonas putida] with FE, BME and NNO 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
Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding., Orville AM, Lipscomb JD, Ohlendorf DH, Biochemistry. 1997 Aug 19;36(33):10052-66. PMID:9254600
Page seeded by OCA on Tue Oct 30 10:21:19 2007
