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.

2hmn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hmn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2hmn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hmn| PDB=2hmn | SCENE= }}
{{STRUCTURE_2hmn| PDB=2hmn | SCENE= }}
-
'''Crystal Structure of the Naphthalene 1,2-Dioxygenase F352V Mutant Bound to Anthracene.'''
+
===Crystal Structure of the Naphthalene 1,2-Dioxygenase F352V Mutant Bound to Anthracene.===
-
==Overview==
+
<!--
-
Rieske oxygenase (RO) systems are two- and three-component enzyme systems that catalyze the formation of cis-dihydrodiols from aromatic substrates. Degradation of pollutants in contaminated soil and generation of chiral synthons have been the major foci of RO research. Substrate specificity and product regio- and stereoselectivity have been shown to vary between individual ROs. While directed evolution methods for altering RO function have been successful in the past, rational engineering of these enzymes still poses a challenge due to the lack of structural understanding. Here we examine the structural changes induced by mutation of Phe-352 in naphthalene 1,2-dioxygenase from Pseudomonas sp. strain NCIB 9816-4 (NDO-O(9816-4)). Structures of the Phe-352-Val mutant in native form and in complex with phenanthrene and anthracene, along with those of wild-type NDO-O(9816-4) in complex with phenanthrene, anthracene, and 3-nitrotoluene, are presented. Phenanthrene was shown to bind in a different orientation in the Phe-352-Val mutant active site from that in the wild type, while anthracene was found to bind in similar positions in both enzymes. Two orientations of 3-nitrotoluene were observed, i.e., a productive and a nonproductive orientation. These orientations help explain why NDO-O(9816-4) forms different products from 3-nitrotoluene than those made from nitrobenzene dioxygenase. Comparison of these structures among themselves and with other known ROs bound to substrates reveals that the orientation of substrate binding at the active site is the primary determinant of product regio- and stereoselectivity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16980501}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16980501 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16980501}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Protien]]
[[Category: Protien]]
[[Category: Rieske oxygenase]]
[[Category: Rieske oxygenase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:27:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:27:56 2008''

Revision as of 04:27, 29 July 2008

Image:2hmn.png

Template:STRUCTURE 2hmn

Crystal Structure of the Naphthalene 1,2-Dioxygenase F352V Mutant Bound to Anthracene.

Template:ABSTRACT PUBMED 16980501

About this Structure

2HMN is a Protein complex structure of sequences from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

Structural basis for regioselectivity and stereoselectivity of product formation by naphthalene 1,2-dioxygenase., Ferraro DJ, Okerlund AL, Mowers JC, Ramaswamy S, J Bacteriol. 2006 Oct;188(19):6986-94. PMID:16980501

Page seeded by OCA on Tue Jul 29 07:27:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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