Arylformamidase: Difference between revisions

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[[Image:Pretty protein.PNG|centre|framed|'''Figure 1.''' ''Arylformamidase'']]
[[Image:Pretty protein.PNG|centre|framed|'''Figure 1.''' ''2PBL'']]


''by Basma Al Alaiwat, Sebastian Mynott and Thomas Parker''
''by Basma Al Alaiwat, Sebastian Mynott and Thomas Parker''
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== Abstract ==
== Abstract ==


2pbl, initially annotated an arylformamidase, was isolated from ''Silibacter sp. TM1040'' and its structure determined by the JCSG. Based on this structure, and using structural, functional and evolutionary analysis, we have further characterised 2pbl. It was found to contain a conserved functional region that is present in a broad range of proteins in many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the HSL family of esterases encompassing a catalytic triad of residues Ser137, Glu215 and His242. Although the specific function is still not known, 2pbl may present novel industrial applications.
2PBL, initially annotated as an arylformamidase, was isolated from ''Silicibacter sp. TM1040'' and its structure determined by the JCSG. Based on structural, functional and evolutionary analysis, we have further characterised 2PBL. It was found to contain a conserved functional region present in A/B-hydrolases of many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the prokaryotic HSL family of esterases. Residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Further experimental characterisation of 2PBL is required to better understand its function.


== Contents ==
== Contents ==

Latest revision as of 03:29, 10 June 2008

Figure 1. 2PBL

by Basma Al Alaiwat, Sebastian Mynott and Thomas Parker

Abstract

2PBL, initially annotated as an arylformamidase, was isolated from Silicibacter sp. TM1040 and its structure determined by the JCSG. Based on structural, functional and evolutionary analysis, we have further characterised 2PBL. It was found to contain a conserved functional region present in A/B-hydrolases of many taxonomic groups. Specifically, it was found to share similar structural and sequence characteristics of the prokaryotic HSL family of esterases. Residues of a probable catalytic triad were identified as Ser137, His242 and Glu215. Further experimental characterisation of 2PBL is required to better understand its function.

Contents

Introduction

Results

Discussion

Methods

Additional Materials

References

Presentations

Sequence & Homology - Sebastian Mynott

Structure - Basma Al Alaiwat

Function - Thomas Parker