4CS0

Direct visualisation of strain-induced protein post-translational modification

Summary for 4CS0

• Entry DOI: 10.2210/pdb4cs0/pdb
• Related: 4CRY 4CRZ
• Descriptor: ASPARTATE 1-DECARBOXYLASE, PANZ, THIOCYANATE ION, ... (6 entities in total)
• Functional Keywords: lyase, coenzyme a, radiation damage, pantothenate
• Biological source: ESCHERICHIA COLI K-12; More
• Cellular location: Cytoplasm : P0A790
• Total number of polymer chains: 2
• Total formula weight: 32410.66

Authors

Monteiro, D.C.F.,Patel, V.,Bartlett, C.P.,Grant, T.D.,Nozaki, S.,Gowdy, J.A.,Snell, E.H.,Niki, H.,Pearson, A.R.,Webb, M.E. (deposition date: 2014-03-02, release date: 2015-03-25, Last modification date: 2024-11-20)

Primary citation

Monteiro, D.C.,Patel, V.,Bartlett, C.P.,Nozaki, S.,Grant, T.D.,Gowdy, J.A.,Thompson, G.S.,Kalverda, A.P.,Snell, E.H.,Niki, H.,Pearson, A.R.,Webb, M.E.
The Structure of the Pand/Panz Protein Complex Reveals Negative Feedback Regulation of Pantothenate Biosynthesis by Coenzyme A.
Chem.Biol., 22:492-, 2015

PubMed Abstract: Coenzyme A (CoA) is an ubiquitous and essential cofactor, synthesized from the precursor pantothenate. Vitamin biosynthetic pathways are normally tightly regulated, including the pathway from pantothenate to CoA. However, no regulation of pantothenate biosynthesis has been identified. We have recently described an additional component in the pantothenate biosynthetic pathway, PanZ, which promotes the activation of the zymogen, PanD, to form aspartate α-decarboxylase (ADC) in a CoA-dependent manner. Here we report the structure of PanZ in complex with PanD, which reveals the structural basis for the CoA dependence of this interaction and activation. In addition, we show that PanZ acts as a CoA-dependent inhibitor of ADC catalysis. This inhibitory effect can effectively regulate the biosynthetic pathway to pantothenate, and thereby also regulate CoA biosynthesis. This represents a previously unobserved mode of metabolic regulation whereby a cofactor-utilizing protein negatively regulates the biosynthesis of the same cofactor.

PubMed: 25910242
DOI: 10.1016/J.CHEMBIOL.2015.03.017

Experimental method

X-RAY DIFFRACTION (2.1 Å)