Journal article
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...
Expand abstract
- Publication status:
- Published
Actions
Access Document
- Publisher copy:
- 10.1110/ps.052002406
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Authors
Bibliographic Details
- Journal:
- Protein science : a publication of the Protein Society
- Volume:
- 15
- Issue:
- 4
- Pages:
- 774-784
- Publication date:
- 2006-04-01
- DOI:
- EISSN:
-
1469-896X
- ISSN:
-
0961-8368
- Source identifiers:
-
72630
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:72630
- UUID:
-
uuid:6a1b7a82-28a2-4a43-bdc3-efc3f760bfc6
- Local pid:
- pubs:72630
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2006
If you are the owner of this record, you can report an update to it here: Report update to this record