2iga

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2iga.gif|left|200px]]
[[Image:2iga.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2iga |SIZE=350|CAPTION= <scene name='initialview01'>2iga</scene>, resolution 1.95&Aring;
+
The line below this paragraph, containing "STRUCTURE_2iga", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=XX2:1-KETO,2-HYDROXY,4-NITROBENZENE,+1+ELECTRON+OXIDIZED'>XX2</scene>, <scene name='pdbligand=XX3:(1S)-1-HYDROPEROXY-1-HYDROXY-2-KETO-5-NITROCYCLOHEXA-3,5-DIENE'>XX3</scene>, <scene name='pdbligand=XXP:2-KETO,5-NITRO,6-HYDROXY-3,5-HEXADIENOIC+ACID'>XXP</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/3,4-dihydroxyphenylacetate_2,3-dioxygenase 3,4-dihydroxyphenylacetate 2,3-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.15 1.13.11.15] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE= hpcd ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=47914 Brevibacterium fuscum])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2iga| PDB=2iga | SCENE= }}
-
|RELATEDENTRY=[[2ig9|2IG9]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iga FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iga OCA], [http://www.ebi.ac.uk/pdbsum/2iga PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iga RCSB]</span>
+
-
}}
+
'''Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.'''
'''Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.'''
Line 28: Line 25:
[[Category: Kovaleva, E G.]]
[[Category: Kovaleva, E G.]]
[[Category: Lipscomb, J D.]]
[[Category: Lipscomb, J D.]]
-
[[Category: alkylperoxo intermediate]]
+
[[Category: Alkylperoxo intermediate]]
-
[[Category: extradiol]]
+
[[Category: Extradiol]]
-
[[Category: fe(ii)]]
+
[[Category: Homoprotocatechuate]]
-
[[Category: homoprotocatechuate]]
+
[[Category: Open-ring product]]
-
[[Category: open-ring product]]
+
[[Category: Oxygenase]]
-
[[Category: oxygenase]]
+
[[Category: Substrate-semiquinone]]
-
[[Category: substrate-semiquinone]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:28:12 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:43:53 2008''
+

Revision as of 04:28, 4 May 2008

Template:STRUCTURE 2iga

Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.


Overview

We report the structures of three intermediates in the O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.

About this Structure

2IGA is a Single protein structure of sequence from Brevibacterium fuscum. Full crystallographic information is available from OCA.

Reference

Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates., Kovaleva EG, Lipscomb JD, Science. 2007 Apr 20;316(5823):453-7. PMID:17446402 Page seeded by OCA on Sun May 4 07:28:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools