Sandbox Reserved 1077

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This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.

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Rv0045c hydrolase from M. Tuberculosis

spinqualitylabelsall models Rv0045c Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Structural highlights The of this enzyme is typical of α/β hydrolases The structure solved by x-ray crystallography[1] was missing the 37 residues as well as a (residues 194-204). A theoretical FALC-loop[2] for this flexible loop is supported by the relative activities of alanine variants of the individual residues 194-204[3].

References

1. ↑ Zheng X, Guo J, Xu L, Li H, Zhang D, Zhang K, Sun F, Wen T, Liu S, Pang H. Crystal Structure of a Novel Esterase Rv0045c from Mycobacterium tuberculosis. PLoS One. 2011;6(5):e20506. Epub 2011 May 26. PMID:21637775 doi:10.1371/journal.pone.0020506
2. ↑ Ko J, Lee D, Park H, Coutsias EA, Lee J, Seok C. The FALC-Loop web server for protein loop modeling. Nucleic Acids Res. 2011 Jul;39(Web Server issue):W210-4. doi: 10.1093/nar/gkr352., Epub 2011 May 16. PMID:21576220 doi:http://dx.doi.org/10.1093/nar/gkr352
3. ↑ Lukowski JK, Savas CP, Gehring AM, McKary MG, Adkins CT, Lavis LD, Hoops GC, Johnson RJ. Distinct substrate selectivity of a metabolic hydrolase from Mycobacterium tuberculosis. Biochemistry. 2014 Dec 2;53(47):7386-95. doi: 10.1021/bi501108u. Epub 2014 Nov, 17. PMID:25354081 doi:http://dx.doi.org/10.1021/bi501108u