1eyr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1eyr.gif|left|200px]]<br /><applet load="1eyr" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1eyr.gif|left|200px]]
-
caption="1eyr, resolution 2.20&Aring;" />
+
 
-
'''Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP'''<br />
+
{{Structure
 +
|PDB= 1eyr |SIZE=350|CAPTION= <scene name='initialview01'>1eyr</scene>, resolution 2.20&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CDP:CYTIDINE-5'-DIPHOSPHATE'>CDP</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/N-acylneuraminate_cytidylyltransferase N-acylneuraminate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.43 2.7.7.43]
 +
|GENE=
 +
}}
 +
 
 +
'''Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1EYR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] with <scene name='pdbligand=CDP:'>CDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/N-acylneuraminate_cytidylyltransferase N-acylneuraminate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.43 2.7.7.43] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYR OCA].
+
1EYR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYR OCA].
==Reference==
==Reference==
-
Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP., Mosimann SC, Gilbert M, Dombroswki D, To R, Wakarchuk W, Strynadka NC, J Biol Chem. 2001 Mar 16;276(11):8190-6. Epub 2000 Dec 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11113120 11113120]
+
Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP., Mosimann SC, Gilbert M, Dombroswki D, To R, Wakarchuk W, Strynadka NC, J Biol Chem. 2001 Mar 16;276(11):8190-6. Epub 2000 Dec 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11113120 11113120]
[[Category: N-acylneuraminate cytidylyltransferase]]
[[Category: N-acylneuraminate cytidylyltransferase]]
[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
Line 25: Line 34:
[[Category: synthetase]]
[[Category: synthetase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:56 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:02:02 2008''

Revision as of 09:02, 20 March 2008


PDB ID 1eyr

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Activity: N-acylneuraminate cytidylyltransferase, with EC number 2.7.7.43
Coordinates: save as pdb, mmCIF, xml



Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP


Overview

The x-ray crystallographic structure of selenomethionyl cytosine-5'-monophosphate-acylneuraminate synthetase (CMP-NeuAc synthetase) from Neisseria meningitidis has been determined at 2.0-A resolution using multiple-wavelength anomalous dispersion phasing, and a second structure, in the presence of the substrate analogue CDP, has been determined at 2.2-A resolution by molecular replacement. This work identifies the active site residues for this class of enzyme for the first time. The detailed interactions between the enzyme and CDP within the mononucleotide-binding pocket are directly observed, and the acylneuraminate-binding pocket has also been identified. A model of acylneuraminate bound to CMP-NeuAc synthetase has been constructed and provides a structural basis for understanding the mechanism of production of "activated" sialic acids. Sialic acids are key saccharide components on the surface of mammalian cells and can be virulence factors in a variety of bacterial species (e.g. Neisseria, Haemophilus, group B streptococci, etc.). As such, the identification of the bacterial CMP-NeuAc synthetase active site can serve as a starting point for rational drug design strategies.

About this Structure

1EYR is a Single protein structure of sequence from Neisseria meningitidis. Full crystallographic information is available from OCA.

Reference

Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP., Mosimann SC, Gilbert M, Dombroswki D, To R, Wakarchuk W, Strynadka NC, J Biol Chem. 2001 Mar 16;276(11):8190-6. Epub 2000 Dec 11. PMID:11113120

Page seeded by OCA on Thu Mar 20 11:02:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools