3VZZ

Crystal structure of PcrB complexed with FsPP from bacillus subtilis subap. subtilis str. 168

Summary for 3VZZ

Entry DOI	10.2210/pdb3vzz/pdb
Related	3VZX 3VZY 3W00 3W01 3W02
Descriptor	Heptaprenylglyceryl phosphate synthase, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywords	biosynthesis, prenyltransferases, enzyme catalysis, transferase
Biological source	Bacillus subtilis
Total number of polymer chains	2
Total formula weight	50739.17
Authors	Ren, F.,Feng, X.,Ko, T.P.,Huang, C.H.,Hu, Y.,Chan, H.C.,Liu, Y.L.,Wang, K.,Chen, C.C.,Pang, X.,He, M.,Li, Y.,Oldfield, E.,Guo, R.T. (deposition date: 2012-10-17, release date: 2012-12-26, Last modification date: 2023-11-08)
Primary citation	Ren, F.,Feng, X.,Ko, T.P.,Huang, C.H.,Hu, Y.,Chan, H.C.,Liu, Y.L.,Wang, K.,Chen, C.C.,Pang, X.,He, M.,Li, Y.,Oldfield, E.,Guo, R.T. Insights into TIM-barrel prenyl transferase mechanisms: crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus Chembiochem, 14:195-199, 2013 Cited by PubMed Abstract: Well structured: As a new triose phosphate isomerase (TIM) barrel-fold prenyl transferase, PcrB catalyzes the production of heptaprenylglyceryl phosphate from heptaprenyl diphosphate and glycerol-1-phosphate. Crystal structures of PcrB from Bacillus subtilis and Staphylococcus aureus in complex with ligands were solved, and together with site-directed mutagenesis and bioinformatics analyses, clearly reveal the catalytic mechanism of the enzyme. PubMed: 23322418 DOI: 10.1002/cbic.201200748 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.04 Å)

Structure validation