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Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding.

Abstract:

Methicillin-resistant Staphylococcus aureus (MRSA) poses a major threat to human health, particularly through hospital acquired infection. The spread of MRSA means that novel targets are required to develop potential inhibitors to combat infections caused by such drug-resistant bacteria. Thymidylate kinase (TMK) is attractive as an antibacterial target as it is essential for providing components for DNA synthesis. Here, we report crystal structures of unliganded and thymidylate-bound forms of...

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Publication status:
Published

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Publisher copy:
10.1110/ps.052002406

Authors


Dhaliwal, B More by this author
Nichols, CE More by this author
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Journal:
Protein science : a publication of the Protein Society
Volume:
15
Issue:
4
Pages:
774-784
Publication date:
2006-04-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:6a1b7a82-28a2-4a43-bdc3-efc3f760bfc6
Source identifiers:
72630
Local pid:
pubs:72630

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