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Rhomboid protease

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== Structural highlights ==
== Structural highlights ==
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The inhibitor isocoumarin binds to the GlpG catalytic residues Ser and His<ref>PMID:20890268</ref>.
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The inhibitor <scene name='55/551211/Cv/3'>isocoumarin covalently binds to the GlpG catalytic residues Ser and His</scene> (in deepskyblue)<ref>PMID:20890268</ref>. <scene name='55/551211/Cv/4'>Whole active site</scene>. Water molecules shown as red spheres.
</StructureSection>
</StructureSection>

Revision as of 11:18, 10 August 2016

Structure of rhomboid protease complex with inhibitor isocoumarin and nonyglucoside detergent molecules (PDB entry 2xow)

Drag the structure with the mouse to rotate

3D Structures of rhomboid protease

Updated on 10-August-2016

References

  1. ↑ Freeman M. Rhomboid proteases and their biological functions. Annu Rev Genet. 2008;42:191-210. doi: 10.1146/annurev.genet.42.110807.091628. PMID:18605900 doi:http://dx.doi.org/10.1146/annurev.genet.42.110807.091628
  2. ↑ Vinothkumar KR, Strisovsky K, Andreeva A, Christova Y, Verhelst S, Freeman M. The structural basis for catalysis and substrate specificity of a rhomboid protease. EMBO J. 2010 Oct 1. PMID:20890268 doi:10.1038/emboj.2010.243

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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