This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3b9n

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3b9n.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3b9n.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3b9n| PDB=3b9n | SCENE= }}
{{STRUCTURE_3b9n| PDB=3b9n | SCENE= }}
-
'''Crystal structure of long-chain alkane monooxygenase (LadA)'''
+
===Crystal structure of long-chain alkane monooxygenase (LadA)===
-
==Overview==
+
<!--
-
LadA, a long-chain alkane monooxygenase, utilizes a terminal oxidation pathway for the conversion of long-chain alkanes (up to at least C(36)) to corresponding primary alcohols in thermophilic bacillus Geobacillus thermodenitrificans NG80-2. Here, we report the first structure of the long-chain alkane hydroxylase, LadA, and its complex with the flavin mononucleotide (FMN) coenzyme. LadA is characterized as a new member of the SsuD subfamily of the bacterial luciferase family via a surprising structural relationship. The LadA:FMN binary complex structure and a LadA:FMN:alkane model reveal a hydrophobic cavity that has dual roles: to provide a hydrogen-bond donor (His138) for catalysis and to create a solvent-free environment in which to stabilize the C4a-hydroperoxyflavin intermediate. Consequently, LadA should catalyze the conversion of long-chain alkanes via the acknowledged flavoprotein monooxygenase mechanism. This finding suggests that the ability of LadA to catalyze the degradation of long-chain alkanes is determined by the binding mode of the long-chain alkane substrates. The LadA structure opens a rational perspective to explore and alter the substrate binding site of LadA, with potential biotechnological applications in areas such as petroleum exploration and treatment of environmental oil pollution.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18164311}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18164311 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18164311}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Plasmid]]
[[Category: Plasmid]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:33:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:21:03 2008''

Revision as of 12:21, 29 July 2008

Template:STRUCTURE 3b9n

Crystal structure of long-chain alkane monooxygenase (LadA)

Template:ABSTRACT PUBMED 18164311

About this Structure

3B9N is a Single protein structure of sequence from Geobacillus thermodenitrificans. Full crystallographic information is available from OCA.

Reference

Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase., Li L, Liu X, Yang W, Xu F, Wang W, Feng L, Bartlam M, Wang L, Rao Z, J Mol Biol. 2008 Feb 15;376(2):453-65. Epub 2007 Nov 28. PMID:18164311

Page seeded by OCA on Tue Jul 29 15:21:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools