1uuw

From Proteopedia

(Difference between revisions)

Revision as of 08:09, 28 March 2018

NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE BOUND IN THE ACTIVE SITE.

Structural highlights

1uuw 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, 1o7p, 1o7w, 1uuv
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

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.

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^[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. NO binding to naphthalene dioxygenase. J Biol Inorg Chem. 2005 Aug;10(5):483-9. Epub 2005 Sep 23. PMID:15942729 doi:http://dx.doi.org/10.1007/s00775-005-0657-1

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE BOUND IN THE ACTIVE SITE.==
 <StructureSection load='1uuw' size='340' side='right' caption='[[1uuw]], [[Resolution|resolution]] 2.30&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]], [[1o7p|1o7p]], [[1o7w|1o7w]], [[1uuv|1uuv]]</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=1uuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uuw OCA], [http://pdbe.org/1uuw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uuw RCSB], [http://www.ebi.ac.uk/pdbsum/1uuw 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=1uuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uuw OCA], [http://pdbe.org/1uuw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uuw RCSB], [http://www.ebi.ac.uk/pdbsum/1uuw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uuw ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uu/1uuw_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uu/1uuw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 44: / Line 45: @@
 [[Category: Parales, R E]]
 [[Category: Ramaswamy, S]]
+[[Category: 2fe-2]]
 [[Category: Aromatic hydrocarbons catabolism]]
 [[Category: Dioxygenase]]
@@ Line 53: / Line 55: @@
 [[Category: Non-heme iron dioxygenase]]
 [[Category: Oxidoreductase]]
+[[Category: Plasmid]]

1uuw

From Proteopedia

Revision as of 08:09, 28 March 2018

NAPHTHALENE 1,2-DIOXYGENASE WITH NITRIC OXIDE BOUND IN THE ACTIVE SITE.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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