Journal article icon

Journal article

Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase.

Abstract:

The X-ray crystal structure of Mycobacterium tuberculosis shikimate kinase (SK) with bound shikimate and adenosine diphosphate (ADP) has been determined to a resolution of 2.15 A. The binding of shikimate in a shikimate kinase crystal structure has not previously been reported. The substrate binds in a pocket lined with hydrophobic residues and interacts with several highly conserved charged residues including Asp34, Arg58, Glu61 and Arg136 which project into the cavity. Comparisons of our te...

Expand abstract
Publication status:
Published

Actions


Access Document


Authors


Journal:
FEBS letters
Volume:
574
Issue:
1-3
Pages:
49-54
Publication date:
2004-09-01
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
Source identifiers:
72622
Language:
English
Keywords:
Pubs id:
pubs:72622
UUID:
uuid:21da1fb7-b47d-4dc2-83a5-f4fd2f0463f4
Local pid:
pubs:72622
Deposit date:
2012-12-19

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP