Publication Date:
2008-06-28
Description:
Nonribosomal peptide synthetases (NRPSs) are modular multidomain enzymes that act as an assembly line to catalyze the biosynthesis of complex natural products. The crystal structure of the 144-kilodalton Bacillus subtilis termination module SrfA-C was solved at 2.6 angstrom resolution. The adenylation and condensation domains of SrfA-C associate closely to form a catalytic platform, with their active sites on the same side of the platform. The peptidyl carrier protein domain is flexibly tethered to this platform and thus can move with its substrate-loaded 4'-phosphopantetheine arm between the active site of the adenylation domain and the donor side of the condensation domain. The SrfA-C crystal structure has implications for the rational redesign of NRPSs as a means of producing novel bioactive peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanovic, Alan -- Samel, Stefan A -- Essen, Lars-Oliver -- Marahiel, Mohamed A -- New York, N.Y. -- Science. 2008 Aug 1;321(5889):659-63. doi: 10.1126/science.1159850. Epub 2008 Jun 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry, Department of Chemistry, Philipps University Marburg, Hans-Meerwein-Strasse, D35032 Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18583577" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Bacillus subtilis/*enzymology
;
Bacterial Proteins/*chemistry/metabolism
;
Binding Sites
;
Catalytic Domain
;
Crystallography, X-Ray
;
Models, Molecular
;
Molecular Sequence Data
;
Peptide Synthases/*chemistry/metabolism
;
Protein Conformation
;
Protein Engineering
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Recombinant Fusion Proteins/chemistry/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
