5GXT

Crystal structure of PigG

Summary for 5GXT

• Entry DOI: 10.2210/pdb5gxt/pdb
• Related: 5GXV
• Descriptor: Maltose-binding periplasmic protein,PigG, MAGNESIUM ION (3 entities in total)
• Functional Keywords: pigg, prodigiosin, protein transport
• Biological source: Escherichia coli; More
• Total number of polymer chains: 1
• Total formula weight: 51415.29

Authors

Zhang, F.,Ran, T.,Xu, D.,Wang, W. (deposition date: 2016-09-20, release date: 2017-07-19, Last modification date: 2024-03-20)

Primary citation

Zhang, F.,Wei, Q.,Tong, H.,Xu, D.,Wang, W.,Ran, T.
Crystal structure of MBP-PigG fusion protein and the essential function of PigG in the prodigiosin biosynthetic pathway in Serratia marcescens FS14.
Int. J. Biol. Macromol., 99:394-400, 2017

PubMed Abstract: Prodigiosin, a tripyrrole red pigment is synthesized by Serratia and some other microbes through a bifurcated biosynthesis pathway; MBC (4-methoxy-2,2'-bipyrrole-5-carbaldehyde) and MAP (2-methyl-3-n-amyl-pyrrole) are synthesized separately and then condensed by PigC to form prodigiosin. PigI, PigG and PigA have been shown to be involved in the first steps of MBC biosynthesis (proline incorporation). The crystal structure of PigG was resolved to elucidate its function and mechanism. PigG, an acyl carrier protein (ACP), features the ACP architecture:, a helical bundle fold containing three major helices and a minor distorted helix together with a conserved "S" motif. An in-frame deletion mutation of the pigG gene abolished the synthesis of prodigiosin in Serratia marcescens FS14. The production of prodigiosin was fully restored by complementation of intact pigG; however the S36A mutant was not able to restore function in the in-frame deletion pigG mutant, indicating that PigG and the conserved serine residue (S36) of PigG are essential for the synthesis of prodigiosin.

PubMed: 28258005
DOI: 10.1016/j.ijbiomac.2017.02.088

Experimental method

X-RAY DIFFRACTION (2.245 Å)