1SBR

The structure and function of B. subtilis YkoF gene product: the complex with thiamin

Summary for 1SBR

• Entry DOI: 10.2210/pdb1sbr/pdb
• Related: 1LXJ 1LXN 1S99
• Descriptor: ykoF, CALCIUM ION, 3-(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-5-(2-HYDROXY-ETHYL)-4-METHYL-THIAZOL-3-IUM, ... (4 entities in total)
• Functional Keywords: ykof, thiamin-binding protein, act-domain family, ligand binding protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 45629.36

Authors

Devedjiev, Y.,Surendranath, Y.,Derewenda, U.,Derewenda, Z.S. (deposition date: 2004-02-11, release date: 2004-10-05, Last modification date: 2024-10-30)

Primary citation

Devedjiev, Y.,Surendranath, Y.,Derewenda, U.,Gabrys, A.,Cooper, D.R.,Zhang, R.G.,Lezondra, L.,Joachimiak, A.,Derewenda, Z.S.
The Structure and Ligand Binding Properties of the B.subtilis YkoF Gene Product, a Member of a Novel Family of Thiamin/HMP-binding Proteins
J.Mol.Biol., 343:395-406, 2004

PubMed Abstract: The crystal structure of the Bacillus subtilis YkoF gene product, a protein involved in the hydroxymethyl pyrimidine (HMP) salvage pathway, was solved by the multiwavelength anomalous dispersion (MAD) method and refined with data extending to 1.65 A resolution. The atomic model of the protein shows a homodimeric association of two polypeptide chains, each containing an internal repeat of a ferredoxin-like betaalphabetabetaalphabeta fold, as seen in the ACT and RAM-domains. Each repeat shows a remarkable similarity to two members of the COG0011 domain family, the MTH1187 and YBL001c proteins, the crystal structures of which were recently solved by the Northeast Structural Genomics Consortium. Two YkoF monomers form a tightly associated dimer, in which the amino acid residues forming the interface are conserved among family members. A putative small-ligand binding site was located within each repeat in a position analogous to the serine-binding site of the ACT-domain of the Escherichia coli phosphoglycerate dehydrogenase. Genetic data suggested that this could be a thiamin or HMP-binding site. Calorimetric data confirmed that YkoF binds two thiamin molecules with varying affinities and a thiamine-YkoF complex was obtained by co-crystallization. The atomic model of the complex was refined using data to 2.3 A resolution and revealed a unique H-bonding pattern that constitutes the molecular basis of specificity for the HMP moiety of thiamin.

PubMed: 15451668
DOI: 10.1016/j.jmb.2004.08.037

Experimental method

X-RAY DIFFRACTION (2.3 Å)