1eil: Difference between revisions
New page: left|200px<br /> <applet load="1eil" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eil, resolution 2.Å" /> '''2,3-DIHYDROXYBIPHENYL... |
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[[Image:1eil.gif|left|200px]]<br /> | [[Image:1eil.gif|left|200px]]<br /><applet load="1eil" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1eil" size=" | |||
caption="1eil, resolution 2.Å" /> | caption="1eil, resolution 2.Å" /> | ||
'''2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE'''<br /> | '''2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE'''<br /> | ||
==Overview== | ==Overview== | ||
BphC derived from Pseudomonas sp. strain KKS102, an extradiol type | 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== | ==About this Structure== | ||
1EIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with SO4 and FE as [http://en.wikipedia.org/wiki/ligands ligands]. 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]]. Active as [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] Full crystallographic information is available from [http:// | 1EIL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FE:'>FE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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]]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIL OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: four repetitions of beta-alpha-beta-beta-beta motifs]] | [[Category: four repetitions of beta-alpha-beta-beta-beta motifs]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:11 2008'' | ||
Revision as of 13:28, 21 February 2008
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2,3-DIHYDROXYBIPHENYL-1,2-DIOXYGENASE
OverviewOverview
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 StructureAbout this Structure
1EIL is a Single protein structure of sequence from Pseudomonas sp. with and as ligands. The following page contains interesting information on the relation of 1EIL with [Topoisomerases]. Active as Biphenyl-2,3-diol 1,2-dioxygenase, with EC number 1.13.11.39 Full crystallographic information is available from OCA.
ReferenceReference
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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