This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3ag5
From Proteopedia
Contents |
Crystal Structure of Pantothenate Synthetase from Staphylococcus aureus
Template:ABSTRACT PUBMED 20568730
Function
[PANC_STAA8] Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate (By similarity).
About this Structure
3ag5 is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus nctc 8325. Full crystallographic information is available from OCA.
See Also
Reference
- Satoh A, Konishi S, Tamura H, Stickland HG, Whitney HM, Smith AG, Matsumura H, Inoue T. Substrate-Induced Closing of the Active Site Revealed by the Crystal Structure of Pantothenate Synthetase from Staphylococcus aureus. Biochemistry. 2010 Jul 8. PMID:20568730 doi:10.1021/bi1004206
Categories: Pantoate--beta-alanine ligase | Staphylococcus aureus subsp. aureus nctc 8325 | Inoue, T. | Konishi, S. | Matsumura, H. | Satoh, A. | Smith, A G. | Stickland, H G. | Tamura, H. | Whitney, H M. | Atp-binding | Atp-dependent enzyme | Ligase | Nucleotide-binding | Open/close mechanism | Pantothenate biosynthesis | Pantothenate synthetase
