Structural highlights
Publication Abstract from PubMed
The crystal structures of CsGST in two different space groups revealed that Asp26 and His79 coordinate a zinc ion. In one space group, His46 of an adjacent molecule participates in the coordination within 2.0A. In the other space group, Asp26, His79 and a water molecule coordinate a zinc ion. The CsGST-D26H structure showed that four histidine residues - His26 and His79 from one molecule and the same residues from a symmetry-related neighboring molecule - coordinate a zinc ion. The coordinated zinc ions are located between two molecules and mediate molecular contacts within the crystal.
Crystal structures of 26kDa Clonorchis sinensis glutathione S-transferase reveal zinc binding and putative metal binding.,Han YH, Hong SJ, Cheong HK, Chung YJ Biochem Biophys Res Commun. 2013 Aug 23;438(2):457-61. doi:, 10.1016/j.bbrc.2013.07.102. Epub 2013 Jul 31. PMID:23916611[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Han YH, Hong SJ, Cheong HK, Chung YJ. Crystal structures of 26kDa Clonorchis sinensis glutathione S-transferase reveal zinc binding and putative metal binding. Biochem Biophys Res Commun. 2013 Aug 23;438(2):457-61. doi:, 10.1016/j.bbrc.2013.07.102. Epub 2013 Jul 31. PMID:23916611 doi:10.1016/j.bbrc.2013.07.102
