1o7p

From Proteopedia

(Difference between revisions)

Revision as of 10:03, 1 November 2017

NAPHTHALENE 1,2-DIOXYGENASE, PRODUCT COMPLEX

Structural highlights

1o7p is a 2 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	1eg9, 1ndo, 1o7g, 1o7h, 1o7m, 1o7n, 1o7w
Activity:	Naphthalene 1,2-dioxygenase, with EC number 1.14.12.12
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Binding 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.

References

↑ Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937 doi:http://dx.doi.org/10.1126/science.1078020

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o7p"

@@ Line 1: / Line 1: @@
 ==NAPHTHALENE 1,2-DIOXYGENASE, PRODUCT COMPLEX==
 <StructureSection load='1o7p' size='340' side='right' caption='[[1o7p]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1eg9|1eg9]], [[1ndo|1ndo]], [[1o7g|1o7g]], [[1o7h|1o7h]], [[1o7m|1o7m]], [[1o7n|1o7n]], [[1o7w|1o7w]]</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 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=1o7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7p OCA], [http://pdbe.org/1o7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7p RCSB], [http://www.ebi.ac.uk/pdbsum/1o7p 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=1o7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7p OCA], [http://pdbe.org/1o7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7p RCSB], [http://www.ebi.ac.uk/pdbsum/1o7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7p ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o7p ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1o7p" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Dioxygenase|Dioxygenase]]
 == References ==
 <references/>

1o7p

From Proteopedia

Revision as of 10:03, 1 November 2017

NAPHTHALENE 1,2-DIOXYGENASE, PRODUCT COMPLEX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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