2r1n: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:2r1n.jpg|left|200px]]
{{Seed}}
[[Image:2r1n.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2r1n|  PDB=2r1n  |  SCENE=  }}  
{{STRUCTURE_2r1n|  PDB=2r1n  |  SCENE=  }}  


'''OpdA from Agrobacterium radiobacter with bound slow substrate diethyl 4-methoxyphenyl phosphate (20h)- 1.7 A'''
===OpdA from Agrobacterium radiobacter with bound slow substrate diethyl 4-methoxyphenyl phosphate (20h)- 1.7 A===




==Overview==
<!--
The mechanism by which the binuclear metallophosphotriesterases (PTEs, E.C. 3.1.8.1) catalyse substrate hydrolysis has been extensively studied. The mu-hydroxo bridge between the metal ions has been proposed to be the initiating nucleophile in the hydrolytic reaction. In contrast, analysis of some biomimetic systems has indicated that mu-hydroxo bridges are often not themselves nucleophiles, but act as general bases for freely exchangeable nucleophilic water molecules. Herein, we present crystallographic analyses of a bacterial PTE from Agrobacterium radiobacter, OpdA, capturing the enzyme-substrate complex during hydrolysis. This model of the Michaelis complex suggests the alignment of the substrate will favour attack from a solvent molecule terminally coordinated to the alpha-metal ion. The bridging of both metal ions by the product, without disruption of the mu-hydroxo bridge, is also consistent with nucleophilic attack occurring from the terminal position. When phosphodiesters are soaked into crystals of OpdA, they coordinate bidentately to the beta-metal ion, displacing the mu-hydroxo bridge. Thus, alternative product-binding modes exist for the PTEs, and it is the bridging mode that appears to result from phosphotriester hydrolysis. Kinetic analysis of the PTE and promiscuous phosphodiesterase activities confirms that the presence of a mu-hydroxo bridge during phosphotriester hydrolysis is correlated with a lower pK(a) for the nucleophile, consistent with a general base function during catalysis.
The line below this paragraph, {{ABSTRACT_PUBMED_18082180}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18082180 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18082180}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Opda]]
[[Category: Opda]]
[[Category: Phosphotriesterase]]
[[Category: Phosphotriesterase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 16:05:33 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:26:41 2008''

Revision as of 06:26, 29 July 2008

File:2r1n.png

Template:STRUCTURE 2r1n

OpdA from Agrobacterium radiobacter with bound slow substrate diethyl 4-methoxyphenyl phosphate (20h)- 1.7 A

Template:ABSTRACT PUBMED 18082180

About this Structure

2R1N is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

Reference

In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase., Jackson CJ, Foo JL, Kim HK, Carr PD, Liu JW, Salem G, Ollis DL, J Mol Biol. 2008 Feb 1;375(5):1189-96. Epub 2007 Nov 1. PMID:18082180

Page seeded by OCA on Tue Jul 29 09:26:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2r1n&oldid=736487"