1bkp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 22: | Line 22: | ||
[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14: | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:55:41 2007'' | ||
Revision as of 15:50, 30 October 2007
|
THERMOSTABLE THYMIDYLATE SYNTHASE A FROM BACILLUS SUBTILIS
OverviewOverview
Unlike all other organisms studied to date, Bacillus subtilis expresses, two different thymidylate synthases: bsTS-A and bsTS-B. bsTS-A displays, enhanced enzymatic and structural thermal stability uncharacteristic of, most TSs. Despite the high level of TS conservation across most species, bsTS-A shares low sequence identity (<40%) with the majority of TSs from, other organisms. This TS and the TSs from Lactococcus lactis and phage, Phi3T-to which it is most similar-have been of interest for some time, since, by structure-based sequence alignment, they appear to lack several, key residues shown by mutagenesis to be essential to enzymatic function, [Greene, P. J., Yu, P. L., Zhao, J., Schiffer, C. A., and Santi, D. (1994), Protein Sci. 3, 1114-6]. In addition, bsTS-A demonstrates ... [(full description)]
About this StructureAbout this Structure
1BKP is a [Single protein] structure of sequence from [Bacillus subtilis]. Active as [Thymidylate synthase], with EC number [2.1.1.45]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis., Stout TJ, Schellenberger U, Santi DV, Stroud RM, Biochemistry. 1998 Oct 20;37(42):14736-47. PMID:9778348
Page seeded by OCA on Tue Oct 30 14:55:41 2007