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Author(s) -
Hoffmann Bernd,
Tollinger Martin,
Konrat Robert,
Huhta Marja,
Marsh E. Neil G.,
Kräutler Bernhard
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010903)2:9<603::aid-cbic603>3.0.co;2-z
Subject(s) - binding site , stereochemistry , cofactor , chemistry , nucleotide , biochemistry , enzyme , gene
The cover picture shows figures from the pertinent stages of a detailed NMR spectroscopic study of the solution structure of the B 12 ‐binding protein MutS, a subunit of the coenzyme‐B 12 ‐dependent glutamate mutase of Clostridium tetanomorphum. A comparison of this first structure of a B 12 ‐binding apoprotein with the crystal structures of related holoenzymes—that is, with bound B 12 cofactor—revealed the essential features of the mechanism of B 12 binding. It showed the major part of MutS to be preorganized for B 12 binding, with the B 12 ‐binding site being highly dynamic and partially formed as a “nascent α helix”. Upon binding the nucleotide moiety of B 12 , the important elements of the binding site appear to become structured, including an α helix that forms one side of the binding cleft accommodating the nucleotide tail of the B 12 cofactor. For more details, see the article by Kräutler and co‐workers on p. 643 ff.