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.

2pae

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pae.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2pae.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pae| PDB=2pae | SCENE= }}
{{STRUCTURE_2pae| PDB=2pae | SCENE= }}
-
'''Structure of a H49N mutant dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from Aneurinibacillus thermoaerophilus in complex with TDP'''
+
===Structure of a H49N mutant dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from Aneurinibacillus thermoaerophilus in complex with TDP===
-
==Overview==
+
<!--
-
The repeating unit of the glycan chain in the S-layer of the bacterium Aneurinibacillus thermoaerophilus L420-91(T) is composed of four alpha-d-rhamnose molecules and two 3-acetamido-3,6-dideoxy-alpha-d-galactose moieties (abbreviated as Fucp3NAc). Formation of the glycan layer requires nucleotide-activated sugars as the donor molecules. Whereas the enzymes involved in the synthesis of GDP-rhamnose have been well characterized, less is known regarding the structures and enzymatic mechanisms of the enzymes required for the production of dTDP-Fucp3NAc. One of the enzymes involved in the biosynthesis of dTDP-Fucp3NAc is a 3,4-ketoisomerase, hereafter referred to as FdtA. Here we describe the first three-dimensional structure of this sugar isomerase complexed with dTDP and solved to 1.5 A resolution. The FdtA dimer assumes an almost jellyfish-like appearance with the sole alpha-helices representing the tentacles. Formation of the FdtA dimer represents a classical example of domain swapping whereby beta-strands 2 and 3 from one subunit form part of a beta-sheet in the second subunit. The active site architecture of FdtA is characterized by a cluster of three histidine residues, two of which, His(49) and His(51), appear to be strictly conserved in the amino acid sequences deposited to date. Site-directed mutagenesis experiments, enzymatic assays, and x-ray crystallographic analyses suggest that His(49) functions as an active site base.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17459872}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17459872 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17459872}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Ketoisomerase]]
[[Category: Ketoisomerase]]
[[Category: S-layer biosynthesis]]
[[Category: S-layer biosynthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:43:27 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:43:55 2008''

Revision as of 04:44, 29 July 2008

Image:2pae.png

Template:STRUCTURE 2pae

Structure of a H49N mutant dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase from Aneurinibacillus thermoaerophilus in complex with TDP

Template:ABSTRACT PUBMED 17459872

About this Structure

2PAE is a Single protein structure of sequence from Aneurinibacillus thermoaerophilus. Full crystallographic information is available from OCA.

Reference

The x-ray structure of dTDP-4-keto-6-deoxy-D-glucose-3,4-ketoisomerase., Davis ML, Thoden JB, Holden HM, J Biol Chem. 2007 Jun 29;282(26):19227-36. Epub 2007 Apr 25. PMID:17459872

Page seeded by OCA on Tue Jul 29 07:43:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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