Sandbox Reserved 1077: Difference between revisions

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==Rv0045c hydrolase from ''M. Tuberculosis''==
==Rv0045c hydrolase from ''M. Tuberculosis''==
<StructureSection load='3P2M' size='340' side='right' caption='Rv0045c' scene=''>
<StructureSection load='3P2M' size='340' side='right' caption='Rv0045c' scene=''>
== Function ==
== Disease ==
== Relevance ==


== Structural highlights ==
== Structural highlights ==
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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] 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> model for this flexible loop is supported by the relative activities of alanine variants of the individual residues 194-204<ref>PMID:25354081</ref>.




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

OCA, Geoffrey C. Hoops