3pcj: Difference between revisions

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==About this Structure==
==About this Structure==
3PCJ 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 INO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase]], 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=3PCJ OCA]].  
3PCJ 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 INO 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=3PCJ 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.]]
Line 27: Line 28:
[[Category: transition-state analog complex]]
[[Category: transition-state analog complex]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:27:07 2007''
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:21:24 2007''

Revision as of 11:16, 30 October 2007

File:3pcj.gif


3pcj, resolution 2.13Å

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STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 2-HYDROXYISONICOTINIC ACID N-OXIDE

OverviewOverview

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 StructureAbout this Structure

3PCJ is a [Protein complex] structure of sequences from [Pseudomonas putida] with FE, BME and INO 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].

ReferenceReference

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

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