1eiq: Difference between revisions
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|PDB= 1eiq |SIZE=350|CAPTION= <scene name='initialview01'>1eiq</scene>, resolution 2.0Å | |PDB= 1eiq |SIZE=350|CAPTION= <scene name='initialview01'>1eiq</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene> | |LIGAND= <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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1dhy|1DHY]], [[1eil|1EIL]], [[1eim|1EIM]], [[1eir|1EIR]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eiq OCA], [http://www.ebi.ac.uk/pdbsum/1eiq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eiq RCSB]</span> | |||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Senda, T.]] | [[Category: Senda, T.]] | ||
[[Category: four repetitions of beta-alpha-beta-beta-beta motif]] | [[Category: four repetitions of beta-alpha-beta-beta-beta motif]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:03:21 2008'' | ||
Revision as of 20:03, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Biphenyl-2,3-diol 1,2-dioxygenase, with EC number 1.13.11.39 | ||||||
| Related: | 1DHY, 1EIL, 1EIM, 1EIR
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1EIQ is a Single protein structure of sequence from Pseudomonas sp.. 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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