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Journal article

High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase.

Abstract:

Two high-resolution structures have been determined for Eschericia coli aspartate beta-semialdehyde dehydrogenase (ecASADH), an enzyme of the aspartate biosynthetic pathway, which is a potential target for novel antimicrobial drugs. Both ASADH structures were of the open form and were refined to 1.95 A and 1.6 A resolution, allowing a more detailed comparison with the closed form of the enzyme than previously possible. A more complex scheme for domain closure is apparent with the subunit bein...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2004.05.073

Authors


Journal:
Journal of molecular biology
Volume:
341
Issue:
3
Pages:
797-806
Publication date:
2004-08-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Source identifiers:
72621
Language:
English
Keywords:
Pubs id:
pubs:72621
UUID:
uuid:42125298-b2df-46c2-9081-bc8ed7e5b4fb
Local pid:
pubs:72621
Deposit date:
2012-12-19

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