3DUV

Crystal structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate in the-configuration

Summary for 3DUV

• Entry DOI: 10.2210/pdb3duv/pdb
• Descriptor: 3-deoxy-manno-octulosonate cytidylyltransferase, 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid, O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: cmp-kdo synthetase, 3-deoxy-manno-octulosonate cytidylyltransferase, 3-deoxy-manno-octulosonate, kdsb, cytoplasm, lipopolysaccharide biosynthesis, nucleotidyltransferase, transferase
• Biological source: Haemophilus influenzae
• Cellular location: Cytoplasm (Potential): P44490
• Total number of polymer chains: 2
• Total formula weight: 59986.77

Authors

Yoon, H.J.,Ku, M.J.,Mikami, B.,Suh, S.W. (deposition date: 2008-07-18, release date: 2008-12-09, Last modification date: 2024-10-09)

Primary citation

Yoon, H.J.,Ku, M.J.,Mikami, B.,Suh, S.W.
Structure of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-manno-octulosonate in the beta-configuration.
Acta Crystallogr.,Sect.D, 64:1292-1294, 2008

PubMed Abstract: 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. CKS is unique to Gram-negative bacteria and is an attractive target for the development of antibacterial agents. The crystal structure of CKS from Haemophilus influenzae in complex with the substrate KDO has been determined at 2.30 A resolution by combining single-wavelength anomalous diffraction and molecular-replacement methods. The two monomers in the asymmetric unit differ in the conformation of their C-terminal alpha-helix (Ala230-Asn254). The KDO bound to the active site exists as the beta-pyranose form in the (5)C(2) chair conformation. The structure of CKS from H. influenzae in complex with KDO will be useful in structure-based inhibitor design.

PubMed: 19018107
DOI: 10.1107/S0907444908036342

Experimental method

X-RAY DIFFRACTION (2.3 Å)