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The <scene name='69/694244/Secondary_structure/1'>secondary structure</scene> of this enzyme is typical of α/β hydrolases
The <scene name='69/694244/Secondary_structure/1'>secondary structure</scene> of this enzyme is typical of α/β hydrolases
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The structure solved by x-ray crystallography<ref>PMID:21637775</ref> was missing the <scene name='69/694244/Glu38/1'>N-terminal</scene> 37 residues as well as a <scene name='69/694244/Glu193_and_arg205/3'>flexible loop</scene> (residues 194-204). A theoretical FALC model for this flexible loop is supported by the relative activities of alanine variants of the individual residues 194-204<ref>PMID:25354081</ref>.
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The structure solved by x-ray crystallography<ref>PMID:21637775</ref> was missing the <scene name='69/694244/Glu38/1'>N-terminal</scene> 37 residues as well as a <scene name='69/694244/Glu193_and_arg205/3'>flexible loop</scene> (residues 194-204). A theoretical FALC[http://falc-loop.seoklab.org/] model for this flexible loop is supported by the relative activities of alanine variants of the individual residues 194-204<ref>PMID:25354081</ref>.

Revision as of 00:21, 1 April 2015

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

Rv0045c

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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. ↑ 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
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