We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2vou

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2vou", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:2vou.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2vou.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vou| PDB=2vou | SCENE= }}
{{STRUCTURE_2vou| PDB=2vou | SCENE= }}
-
'''STRUCTURE OF 2,6-DIHYDROXYPYRIDINE-3-HYDROXYLASE FROM ARTHROBACTER NICOTINOVORANS'''
+
===STRUCTURE OF 2,6-DIHYDROXYPYRIDINE-3-HYDROXYLASE FROM ARTHROBACTER NICOTINOVORANS===
-
==Overview==
+
<!--
-
The enzyme 2,6-dihydroxypyridine-3-hydroxylase catalyzes the sixth step of the nicotine degradation pathway in Arthrobacter nicotinovorans. The enzyme was produced in Escherichia coli, purified and crystallized. The crystal structure was solved at 2.6 A resolution, revealing a significant structural relationship with the family of FAD-dependent aromatic hydroxylases, but essentially no sequence homology. The structure was aligned with those of the established family members, showing that the FAD molecules are bound at virtually identical locations. The reported enzyme is a dimer like most other family members, but its dimerization contact differs from the others. The binding position of NAD(P)H to this enzyme family is not clear. Since the reported enzyme accepts only NADH for flavin reduction in contrast to the other established members using NADPH, we searched through the structural alignment and found an indication for the position of the 2'-phosphate of NADPH that is in general agreement with mutational studies on a related enzyme, but contradicts a crystal soaking experiment. Using a bound glycerol molecule and the known substrate positions of three related enzymes as a guide, the substrate 2,6-dihydroxypyridine was placed into the active center. The access to the binding site is discussed. The new active center geometry introduces constraints that render some reaction scenarios more likely than others. It suggests that flavin is reduced at its out-position and then drawn into its in-position, where it binds molecular oxygen. The geometry is consistent with the proposal that peroxy-flavin is protonated by the solvent to yield the electrophilic hydroperoxy-flavin. The substrate is activated by two buried histidines but there is no appropriate base to store the surplus proton of the hydroxylated carbon atom. The implications of this problem are discussed.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18440023}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18440023 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18440023}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Plasmid]]
[[Category: Plasmid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:27:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:21:20 2008''

Revision as of 00:21, 28 July 2008

Image:2vou.png

Template:STRUCTURE 2vou

STRUCTURE OF 2,6-DIHYDROXYPYRIDINE-3-HYDROXYLASE FROM ARTHROBACTER NICOTINOVORANS

Template:ABSTRACT PUBMED 18440023

About this Structure

2VOU is a Single protein structure of sequence from Arthrobacter nicotinovorans. Full crystallographic information is available from OCA.

Reference

Structure of 2,6-dihydroxypyridine 3-hydroxylase from a nicotine-degrading pathway., Treiber N, Schulz GE, J Mol Biol. 2008 May 23;379(1):94-104. Epub 2008 Mar 26. PMID:18440023

Page seeded by OCA on Mon Jul 28 03:21:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vou"
Personal tools