Topological chirality of iron-sulfur proteins.

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

Biopolymers

journal_title

Biopolymers

authors

Liang C,Mislow K

doi

10.1002/(SICI)1097-0282(19971005)42:4<411::AID-BIP

subject

Has Abstract

pub_date

1997-10-05 00:00:00

pages

411-4

issue

4

eissn

0006-3525

issn

1097-0282

pii

10.1002/(SICI)1097-0282(19971005)42:4<411::AID-BIP

journal_volume

42

pub_type

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