1ulj

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[[Image:1ulj.gif|left|200px]]
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[[Image:1ulj.png|left|200px]]
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{{STRUCTURE_1ulj| PDB=1ulj | SCENE= }}
{{STRUCTURE_1ulj| PDB=1ulj | SCENE= }}
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'''Biphenyl dioxygenase (BphA1A2) in complex with the substrate'''
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===Biphenyl dioxygenase (BphA1A2) in complex with the substrate===
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==Overview==
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Biphenyl dioxygenase is the enzyme that catalyzes the stereospecific dioxygenation of the aromatic ring. This enzyme has attracted the attention of researchers due to its ability to oxidize polychlorinated biphenyls, which is one of the serious environmental contaminants. We determined the crystal structure of the terminal oxygenase component of the biphenyl dioxygenase (BphA1A2) derived from Rhodococcus strain sp. RHA1 in substrate-free and complex forms. These crystal structures revealed that the substrate-binding pocket makes significant conformational changes upon substrate binding to accommodate the substrate into the pocket. Our analysis of the crystal structures suggested that the residues in the substrate-binding pocket can be classified into three groups, which, respectively, seem to be responsible for the catalytic reaction, the orientation/conformation of the substrate, and the conformational changes of the substrate-binding pocket. The cooperative actions of residues in the three groups seem to determine the substrate specificity of the enzyme.
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The line below this paragraph, {{ABSTRACT_PUBMED_15342255}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15342255 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15342255}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1., Furusawa Y, Nagarajan V, Tanokura M, Masai E, Fukuda M, Senda T, J Mol Biol. 2004 Sep 17;342(3):1041-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15342255 15342255]
Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1., Furusawa Y, Nagarajan V, Tanokura M, Masai E, Fukuda M, Senda T, J Mol Biol. 2004 Sep 17;342(3):1041-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15342255 15342255]
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Crystallization of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1., Nagarajan V, Sakurai N, Kubota M, Nonaka T, Nagumo H, Takeda H, Nishizaki T, Masai E, Fukuda M, Mitsui Y, Senda T, Protein Pept Lett. 2003 Aug;10(4):412-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14529495 14529495]
[[Category: Biphenyl 2,3-dioxygenase]]
[[Category: Biphenyl 2,3-dioxygenase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Tanokura, M.]]
[[Category: Tanokura, M.]]
[[Category: Alpha3 beta3 hetero hexamer]]
[[Category: Alpha3 beta3 hetero hexamer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:23:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:37:03 2008''

Revision as of 22:37, 27 July 2008

Image:1ulj.png

Template:STRUCTURE 1ulj

Biphenyl dioxygenase (BphA1A2) in complex with the substrate

Template:ABSTRACT PUBMED 15342255

About this Structure

1ULJ is a Protein complex structure of sequences from Rhodococcus sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1., Furusawa Y, Nagarajan V, Tanokura M, Masai E, Fukuda M, Senda T, J Mol Biol. 2004 Sep 17;342(3):1041-52. PMID:15342255

Crystallization of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1., Nagarajan V, Sakurai N, Kubota M, Nonaka T, Nagumo H, Takeda H, Nishizaki T, Masai E, Fukuda M, Mitsui Y, Senda T, Protein Pept Lett. 2003 Aug;10(4):412-7. PMID:14529495

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