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Structural and mechanistic studies of the orf12 gene product from the clavulanic acid biosynthesis pathway.

Abstract:

Structural and biochemical studies of the orf12 gene product (ORF12) from the clavulanic acid (CA) biosynthesis gene cluster are described. Sequence and crystallographic analyses reveal two domains: a C-terminal penicillin-binding protein (PBP)/β-lactamase-type fold with highest structural similarity to the class A β-lactamases fused to an N-terminal domain with a fold similar to steroid isomerases and polyketide cyclases. The C-terminal domain of ORF12 did not show β-lactamase or PBP activit...

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Publication status:
Published

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Publisher copy:
10.1107/s0907444913011013

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Journal:
Acta crystallographica. Section D, Biological crystallography More from this journal
Volume:
69
Issue:
Pt 8
Pages:
1567-1579
Publication date:
2013-08-01
DOI:
EISSN:
1399-0047
ISSN:
0907-4449
Language:
English
Keywords:
Pubs id:
pubs:416489
UUID:
uuid:231f8ddc-ecf5-4f2a-9743-ee6d1f7198f1
Local pid:
pubs:416489
Source identifiers:
416489
Deposit date:
2013-11-16

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