1lrz
From Proteopedia
(New page: 200px<br /><applet load="1lrz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lrz, resolution 2.10Å" /> '''x-ray crystal struct...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1lrz.jpg|left|200px]]<br /><applet load="1lrz" size=" | + | [[Image:1lrz.jpg|left|200px]]<br /><applet load="1lrz" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lrz, resolution 2.10Å" /> | caption="1lrz, resolution 2.10Å" /> | ||
'''x-ray crystal structure of staphylococcus aureus femA'''<br /> | '''x-ray crystal structure of staphylococcus aureus femA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The latter stages of peptidoglycan biosynthesis in Staphylococci involve | + | The latter stages of peptidoglycan biosynthesis in Staphylococci involve the synthesis of a pentaglycine bridge on the epsilon amino group of the pentapeptide lysine side chain. Genetic and biochemical evidence suggest that sequential addition of these glycines is catalyzed by three homologous enzymes, FemX (FmhB), FemA, and FemB. The first protein structure from this family, Staphylococcus aureus FemA, has been solved at 2.1 A resolution by X-ray crystallography. The FemA structure reveals a unique organization of several known protein folds involved in peptide and tRNA binding. The surface of the protein also reveals an L-shaped channel suitable for a peptidoglycan substrate. Analysis of the structural features of this enzyme provides clues to the mechanism of action of S. aureus FemA. |
==About this Structure== | ==About this Structure== | ||
| - | 1LRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http:// | + | 1LRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LRZ OCA]. |
==Reference== | ==Reference== | ||
| Line 27: | Line 27: | ||
[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:01 2008'' |
Revision as of 11:48, 21 February 2008
|
x-ray crystal structure of staphylococcus aureus femA
Overview
The latter stages of peptidoglycan biosynthesis in Staphylococci involve the synthesis of a pentaglycine bridge on the epsilon amino group of the pentapeptide lysine side chain. Genetic and biochemical evidence suggest that sequential addition of these glycines is catalyzed by three homologous enzymes, FemX (FmhB), FemA, and FemB. The first protein structure from this family, Staphylococcus aureus FemA, has been solved at 2.1 A resolution by X-ray crystallography. The FemA structure reveals a unique organization of several known protein folds involved in peptide and tRNA binding. The surface of the protein also reveals an L-shaped channel suitable for a peptidoglycan substrate. Analysis of the structural features of this enzyme provides clues to the mechanism of action of S. aureus FemA.
About this Structure
1LRZ is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of Staphylococcus aureus FemA., Benson TE, Prince DB, Mutchler VT, Curry KA, Ho AM, Sarver RW, Hagadorn JC, Choi GH, Garlick RL, Structure. 2002 Aug;10(8):1107-15. PMID:12176388
Page seeded by OCA on Thu Feb 21 13:48:01 2008
