3iml
From Proteopedia
Contents |
Crystal Structure Of S-Adenosylmethionine Synthetase From Burkholderia Pseudomallei
Template:ABSTRACT PUBMED 23382856
Function
[METK_BURPS] Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme (By similarity).
About this Structure
3iml is a 4 chain structure with sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA.
See Also
Reference
- Baugh L, Gallagher LA, Patrapuvich R, Clifton MC, Gardberg AS, Edwards TE, Armour B, Begley DW, Dieterich SH, Dranow DM, Abendroth J, Fairman JW, Fox D 3rd, Staker BL, Phan I, Gillespie A, Choi R, Nakazawa-Hewitt S, Nguyen MT, Napuli A, Barrett L, Buchko GW, Stacy R, Myler PJ, Stewart LJ, Manoil C, Van Voorhis WC. Combining functional and structural genomics to sample the essential Burkholderia structome. PLoS One. 2013;8(1):e53851. doi: 10.1371/journal.pone.0053851. Epub 2013 Jan 31. PMID:23382856 doi:http://dx.doi.org/10.1371/journal.pone.0053851
Categories: Burkholderia pseudomallei | Methionine adenosyltransferase | Staker, B L. | Atp-binding | Cobalt | Magnesium | Metal-binding | Nucleotide-binding | One-carbon metabolism | Potassium | S-adenosylmethionine synthetase | Seattle structural genomics center for infectious disease | Ssgcid | Structural genomic | Transferase