1eil
From Proteopedia
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| - | [[Image:1eil.gif|left|200px]] | + | [[Image:1eil.gif|left|200px]] |
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| - | '''2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE''' | + | {{Structure |
| + | |PDB= 1eil |SIZE=350|CAPTION= <scene name='initialview01'>1eil</scene>, resolution 2.Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Biphenyl-2,3-diol_1,2-dioxygenase Biphenyl-2,3-diol 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.39 1.13.11.39] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EIL is a [ | + | 1EIL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. The following page contains interesting information on the relation of 1EIL with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb73_1.html Topoisomerases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIL OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase., Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y, J Inorg Biochem. 2001 Feb;83(4):269-79. PMID:[http:// | + | Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase., Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y, J Inorg Biochem. 2001 Feb;83(4):269-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11293547 11293547] |
[[Category: Biphenyl-2,3-diol 1,2-dioxygenase]] | [[Category: Biphenyl-2,3-diol 1,2-dioxygenase]] | ||
[[Category: Pseudomonas sp.]] | [[Category: Pseudomonas sp.]] | ||
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[[Category: FE]] | [[Category: FE]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| - | [[Category: four repetitions of beta-alpha-beta-beta-beta | + | [[Category: four repetitions of beta-alpha-beta-beta-beta motif]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:56:05 2008'' |
Revision as of 08:56, 20 March 2008
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| , resolution 2.Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Biphenyl-2,3-diol 1,2-dioxygenase, with EC number 1.13.11.39 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE
Overview
BphC derived from Pseudomonas sp. strain KKS102, an extradiol type catecholic dioxygenase, is a non-heam iron-containing enzyme, playing an important role in the degradation of biphenyl/PCB (Poly Chlorinated Biphenyls) in the microbe. Although we had earlier solved the crystal structure of KKS102 BphC, it was the inactive form with Fe(III) in the active site. In order to determine the active form structure, BphC was re-activated by anaerobic incubation with Fe(II) and ascorbate, and crystallized anaerobically. The crystal structures of activated BphC and its substrate complex (E x S complex) were determined at 2.0 A resolution under cryogenic condition. In addition, crystal structures of unactivated BphC in substrate free and complex forms were also re-determined. Comparison of activated and unactivated E x S complexes reveals that the orientation of the bound substrate in the active site is significantly different between the two. The structural comparison of the substrate free and complex forms of activated BphC show certain small conformational shifts around the active site upon substrate binding. As a result of the conformational shifts, His194, which has been suggested as the catalytic base, takes part in a weak hydrogen bond with hydroxyl group of the substrate.
About this Structure
1EIL is a Single protein structure of sequence from Pseudomonas sp.. The following page contains interesting information on the relation of 1EIL with [Topoisomerases]. Full crystallographic information is available from OCA.
Reference
Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase., Uragami Y, Senda T, Sugimoto K, Sato N, Nagarajan V, Masai E, Fukuda M, Mitsu Y, J Inorg Biochem. 2001 Feb;83(4):269-79. PMID:11293547
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