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.
4h2w
From Proteopedia
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:023541895</ref><references group="xtra"/><references/> |
[[Category: Agrobacterium fabrum str. c58]] | [[Category: Agrobacterium fabrum str. c58]] | ||
[[Category: Bradyrhizobium japonicum usda 110]] | [[Category: Bradyrhizobium japonicum usda 110]] | ||
Revision as of 16:31, 19 June 2013
Contents |
Crystal structure of engineered Bradyrhizobium japonicum glycine:[carrier protein] ligase complexed with carrier protein from Agrobacterium tumefaciens and AMP
Template:ABSTRACT PUBMED 23541895
Function
[AACL1_BRAJA] Catalyzes the ATP-dependent activation of L-glycine and its transfer to the phosphopantetheine prosthetic group covalently attached to the vicinal carrier protein bsr0959 of yet unknown function. May participate in nonribosomal peptide synthesis or related processes. L-alanine is a poor substrate whereas L-serine or D-amino acids are not substrates for ATP-dependent activation. Does not display tRNA aminoacylation activity. [AACP_AGRT5] Aminoacyl carrier protein. Can be charged with L-alanine, L-glycine or L-serine, via the formation of a thioester bond between the amino acid and the 4'-phosphopantetheinyl prosthetic group, catalyzed by the Atu2573 ligase.
About this Structure
4h2w is a 4 chain structure with sequence from Agrobacterium fabrum str. c58 and Bradyrhizobium japonicum usda 110. Full crystallographic information is available from OCA.
Reference
- Mocibob M, Ivic N, Luic M, Weygand-Durasevic I. Adaptation of Aminoacyl-tRNA Synthetase Catalytic Core to Carrier Protein Aminoacylation. Structure. 2013 Mar 26. pii: S0969-2126(13)00058-0. doi:, 10.1016/j.str.2013.02.017. PMID:23541895 doi:10.1016/j.str.2013.02.017
