1tmx: Difference between revisions

Revision as of 00:57, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tmx.png

Template:STRUCTURE 1tmx

Crystal structure of hydroxyquinol 1,2-dioxygenase from Nocardioides Simplex 3ECrystal structure of hydroxyquinol 1,2-dioxygenase from Nocardioides Simplex 3E

Template:ABSTRACT PUBMED 15772073

About this StructureAbout this Structure

1TMX is a Single protein structure of sequence from Pimelobacter simplex. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation., Ferraroni M, Seifert J, Travkin VM, Thiel M, Kaschabek S, Scozzafava A, Golovleva L, Schlomann M, Briganti F, J Biol Chem. 2005 Jun 3;280(22):21144-54. Epub 2005 Mar 16. PMID:15772073

Page seeded by OCA on Mon Jul 28 00:57:31 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1tmx.gif|left|200px]]
+{{Seed}}
+[[Image:1tmx.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1tmx|  PDB=1tmx  |  SCENE=  }}
-'''Crystal structure of hydroxyquinol 1,2-dioxygenase from Nocardioides Simplex 3E'''
+===Crystal structure of hydroxyquinol 1,2-dioxygenase from Nocardioides Simplex 3E===
-==Overview==
+<!--
-Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2,4-trihydroxybenzene), a central intermediate in the degradation of aromatic compounds including a variety of particularly recalcitrant polychloro- and nitroaromatic pollutants. We report here the primary sequence determination and the analysis of the crystal structure of the 1,2-HQD from Nocardioides simplex 3E solved at 1.75 A resolution using the multiple wavelength anomalous dispersion of the two catalytic irons (1 Fe/293 amino acids). The catalytic Fe(III) coordination polyhedron composed by the side chains of Tyr164, Tyr197, His221, and His223 resembles that of the other known intradiol-cleaving dioxygenases, but several of the tertiary structure features are notably different. One of the most distinctive characteristics of the present structure is the extensive openings and consequent exposure to solvent of the upper part of the catalytic cavity arranged to favor the binding of hydroxyquinols but not catechols. A co-crystallized benzoate-like molecule is also found bound to the metal center forming a distinctive hydrogen bond network as observed previously also in 4-chlorocatechol 1,2-dioxygenase from Rhodococcus opacus 1CP. This is the first structure of an intradiol dioxygenase specialized in hydroxyquinol ring cleavage to be investigated in detail.
+The line below this paragraph, {{ABSTRACT_PUBMED_15772073}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15772073 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15772073}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Travkin, V M.]]
 [[Category: Beta barrel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:08:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:57:31 2008''