1o7h: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1o7h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7H FirstGlance]. <br> | <table><tr><td colspan='2'>[[1o7h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7H FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eg9|1eg9]], [[1ndo|1ndo]], [[1o7g|1o7g]], [[1o7m|1o7m]], [[1o7n|1o7n]], [[1o7p|1o7p]], [[1o7w|1o7w]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eg9|1eg9]], [[1ndo|1ndo]], [[1o7g|1o7g]], [[1o7m|1o7m]], [[1o7n|1o7n]], [[1o7p|1o7p]], [[1o7w|1o7w]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7h RCSB], [http://www.ebi.ac.uk/pdbsum/1o7h PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7h RCSB], [http://www.ebi.ac.uk/pdbsum/1o7h PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/NDOB_PSEPU NDOB_PSEPU]] Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol. [[http://www.uniprot.org/uniprot/NDOC_PSEPU NDOC_PSEPU]] Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol. The beta subunit may be responsible for the substrate specificity of the enzyme. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Naphthalene 1,2-dioxygenase]] | [[Category: Naphthalene 1,2-dioxygenase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
[[Category: Eklund, H | [[Category: Eklund, H]] | ||
[[Category: Gibson, D T | [[Category: Gibson, D T]] | ||
[[Category: Karlsson, A | [[Category: Karlsson, A]] | ||
[[Category: Parales, J V | [[Category: Parales, J V]] | ||
[[Category: Parales, R E | [[Category: Parales, R E]] | ||
[[Category: Ramaswamy, S | [[Category: Ramaswamy, S]] | ||
[[Category: Aromatic hydrocarbon catabolism]] | [[Category: Aromatic hydrocarbon catabolism]] | ||
[[Category: Enzyme-substrate complex]] | [[Category: Enzyme-substrate complex]] | ||
Revision as of 18:37, 25 December 2014
NAPHTHALENE 1,2-DIOXYGENASE WITH OXIDIZED RIESKE IRON SULPHUR CENTER SITE.NAPHTHALENE 1,2-DIOXYGENASE WITH OXIDIZED RIESKE IRON SULPHUR CENTER SITE.
Structural highlights
Function[NDOB_PSEPU] Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol. [NDOC_PSEPU] Component of the naphthalene dioxygenase (NDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into naphthalene to form cis-naphthalene dihydrodiol. The beta subunit may be responsible for the substrate specificity of the enzyme. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBinding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron.,Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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