Abstract:
:An examination of x-ray structures of single-cluster [4Fe-4S] proteins in the Protein Data Bank has revealed that all redox proteins and the glutamine 5-phosphoribosyl-l-pyrophosphate amidotransferase from Bacillus subtilis have a topological configuration arbitrarily designated as D, whereas the DNA repair enzyme endonuclease III from Escherichia coli has the opposite topological configuration L. This is the first example in which both senses of topological chirality have been observed in a class of proteins.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Liang C,Mislow Kdoi
10.1002/(SICI)1097-0282(19971005)42:4<411::AID-BIPsubject
Has Abstractpub_date
1997-10-05 00:00:00pages
411-4issue
4eissn
0006-3525issn
1097-0282pii
10.1002/(SICI)1097-0282(19971005)42:4<411::AID-BIPjournal_volume
42pub_type
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