Sandbox Reserved 1077: Difference between revisions

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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. TuberculosisRv0045c hydrolase from M. Tuberculosis

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].

ReferencesReferences

↑ 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
↑ 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
↑ 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Geoffrey C. Hoops

[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

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Revision as of 03:27, 1 April 2015 view source Geoffrey C. Hoops (talk \| contribs) 208 edits No edit summary ← Older edit		Revision as of 03:51, 1 April 2015 view source Geoffrey C. Hoops (talk \| contribs) 208 edits No edit summary Newer edit →
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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

	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 [http://falc-loop.seoklab.org/ FALC-loop]<ref>PMID:21576220</ref> model for this flexible loop is supported by the relative activities of alanine variants of the individual residues 194-204<ref>PMID:25354081</ref>.		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 [http://falc-loop.seoklab.org/ FALC-loop]<ref>PMID:21576220</ref> <scene name='69/694244/Loop_modeled_backbone_view/1'>model</scene>for this flexible loop is supported by the relative activities of alanine variants of the individual residues 194-204<ref>PMID:25354081</ref>.