To see full content of that page you need the activeISee plugin.
Get the latest version from here.

Structure of IDP02355

3-deoxy-manno-octulosonate cytidylyltransferase from Yersinia pestis.

Edit deposit information
CSGID target
IDP02355 
PDB Id
3JTJ (NCBI MMDB
Authors
J.Osipiuk,M.Zhou,S.Grimshaw,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Sep 12, 2009 
Release Date
Sep 22, 2009 

Annotation

Description
The enzyme 3-deoxy-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase; CKS) catalyzes the activation of 3-deoxy-D-manno-octulosonate (or 2-keto-3-deoxy-manno-octonic acid; KDO) by forming CMP-KDO. The enzymes belong to cytidylyltransferase protein family being a part of GT-A clan that contains diverse glycosyltransferases that possess a Rossmann like fold. KDO is an essential component of lipopolysaccharides (LPS) in Gram-negative bacteria. Incorporation of KDO into LPS requires its activation by 3-deoxy-manno-octulosonate CKS. The Yesinia pestis enzyme coded by kdsB gene is 77% identical to its E.coli homolog. Two isozymes of CKS have been found in Escherichia coli. One of them, named L-CKS, is encoded by the kdsB gene and participates in the biosynthesis of LPS. The other isozyme, K-CKS, is encoded by the kpsU gene and is involved in capsule expression. CKS is unique to Gram-negative bacteria and is absent from mammalian cells. Therefore, CKS is an attractive target for the development of antibacterial agents. 
Functional assignment
 

Ligands

Ligand code Name Ligand type
IMD
MSE SELENOMETHIONINE modified residue

Structure information

Unit cell parameters

Space Group
P 32 2 1  
Unit Cell

a=97.06Å, b=97.06Å, c=93.63Å
α=90.00, β=90.00, γ=120.00 
Solvent content
73.02  
Matthews coefficient
4.56  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
43.20-2.18Å (2.24-2.18Å)  
Rall(%)
18.3 
Rwork(%)
18.2 (24.3) 
Rfree(%)
20.9 (30.6) 
Num. observed reflections
28162 (1803) 
Num. Rfree reflections
1408 (80) 
Completeness(%)
99.4 (91.8) 

Model parameters

Num Atoms
1882  
Num Waters
112  
Num Hetatoms
167  
Model mean isotropic B factor
39.690Å2  
RMSD bond length
0.019Å  
RMSD bond angle
1.565°  
Filename uploaded
rcsb055140.pdb (uploaded on Sep 16, 2009 4:54 PM)  
Inserted
Sep 16, 2009