1IHO

CRYSTAL APO-STRUCTURE OF PANTOTHENATE SYNTHETASE FROM E. COLI

Summary for 1IHO

• Entry DOI: 10.2210/pdb1iho/pdb
• Descriptor: PANTOATE--BETA-ALANINE LIGASE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: rossmann fold, dimer, apo, high, ksmks, flexible domains, multidomain, ligase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 63525.66

Authors

von Delft, F.,Lewendon, A.,Dhanaraj, V.,Blundell, T.L.,Abell, C.,Smith, A. (deposition date: 2001-04-19, release date: 2001-05-30, Last modification date: 2024-04-03)

Primary citation

von Delft, F.,Lewendon, A.,Dhanaraj, V.,Blundell, T.L.,Abell, C.,Smith, A.G.
The crystal structure of E. coli pantothenate synthetase confirms it as a member of the cytidylyltransferase superfamily.
Structure, 9:439-450, 2001

PubMed Abstract: Pantothenate synthetase (EC 6.3.2.1) is the last enzyme of the pathway of pantothenate (vitamin B(5)) synthesis. It catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction.

PubMed: 11377204
DOI: 10.1016/S0969-2126(01)00604-9

Experimental method

X-RAY DIFFRACTION (1.7 Å)