3DMS

1.65A crystal structure of isocitrate dehydrogenase from Burkholderia pseudomallei

Summary for 3DMS

• Entry DOI: 10.2210/pdb3dms/pdb
• Descriptor: Isocitrate dehydrogenase [NADP] (2 entities in total)
• Functional Keywords: burkholderia, pseudomallei, isocitrate, dehydrogenase, structural genomics, seattle structural genomics center for infectious disease, ssgcid, glyoxylate bypass, manganese, metal-binding, nadp, oxidoreductase, tricarboxylic acid cycle
• Biological source: Burkholderia pseudomallei (Pseudomonas pseudomallei)
• Total number of polymer chains: 1
• Total formula weight: 47231.09

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2008-07-01, release date: 2008-07-15, Last modification date: 2024-02-21)

Primary citation

Yates, S.P.,Edwards, T.E.,Bryan, C.M.,Stein, A.J.,Van Voorhis, W.C.,Myler, P.J.,Stewart, L.J.,Zheng, J.,Jia, Z.
Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.
Biochemistry, 50:8103-8106, 2011

PubMed Abstract: Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhibits the necessary structural elements required for AceK recognition. Kinetic analyses provided further confirmation that Bp-ICDH is a substrate for AceK. We conclude that the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria.

PubMed: 21870819
DOI: 10.1021/bi200809p

Experimental method

X-RAY DIFFRACTION (1.65 Å)