1uuv
From Proteopedia
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| - | [[Image:1uuv.gif|left|200px]]<br /><applet load="1uuv" size=" | + | [[Image:1uuv.gif|left|200px]]<br /><applet load="1uuv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uuv, resolution 1.65Å" /> | caption="1uuv, resolution 1.65Å" /> | ||
'''NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE AND INDOLE BOUND IN THE ACTIVE SITE.'''<br /> | '''NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE AND INDOLE BOUND IN THE ACTIVE SITE.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UUV 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, SO4, FES, EDO, IND and NO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Naphthalene_1,2-dioxygenase Naphthalene 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | + | 1UUV 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 <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FES:'>FES</scene>, <scene name='pdbligand=EDO:'>EDO</scene>, <scene name='pdbligand=IND:'>IND</scene> and <scene name='pdbligand=NO:'>NO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Naphthalene_1,2-dioxygenase Naphthalene 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12] Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UUV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:08:14 2008'' |
Revision as of 08:08, 3 February 2008
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NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE AND INDOLE BOUND IN THE ACTIVE SITE.
Overview
Nitric oxide (NO) is commonly used as an analogue for dioxygen in, structural and spectroscopic studies of oxygen binding and oxygen, activation. In this study, crystallographic structures of naphthalene, dioxygenase (NDO) in complex with nitric oxide are reported. In the, presence of the aromatic substrate indole, NO is bound end-on to the, active-site mononuclear iron of NDO. The structural observations correlate, well with spectroscopic measurements of NO binding to NDO in solution., However, the end-on binding of NO is in contrast to the recently reported, structure of oxygen to the active-site iron of NDO that binds side-on., While NO is a good oxygen analogue with many similarities to O(2), the, different binding mode of NO to the active-site iron atom leads to, different mechanistic implications. Hence, caution needs to be used in, extrapolating NO as an analogue to O(2) binding.
About this Structure
1UUV is a Protein complex structure of sequences from Pseudomonas putida with , , , , and as ligands. Active as Naphthalene 1,2-dioxygenase, with EC number 1.14.12.12 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
NO binding to naphthalene dioxygenase., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, J Biol Inorg Chem. 2005 Aug;10(5):483-9. Epub 2005 Sep 23. PMID:15942729
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Categories: Naphthalene 1,2-dioxygenase | Protein complex | Pseudomonas putida | Eklund, H. | Gibson, D.T. | Karlsson, A. | Parales, J.V. | Parales, R.E. | Ramaswamy, S. | EDO | FE | FES | IND | NO | SO4 | Aromatic hydrocarbons catabolism | Enzyme-substrate complex | Non-heme iron dioxygenase | Oxidoreductase
