التفاصيل البيبلوغرافية
| العنوان: |
The hypothetical periplasmic protein PA1624 from Pseudomonas aeruginosa folds into a unique two domain structure |
| المؤلفون: |
Feiler, C.G., Weiss, M.S., Blankenfeldt, W. |
| سنة النشر: |
2020 |
| المجموعة: |
Helmholtz Zentrum Berlin (HZB): Publications |
| مصطلحات موضوعية: |
Inhouse research on structure dynamics and function of matter |
| الوصف: |
The crystal structure of the 268 residue periplasmic protein PA1624 from the opportunistic pathogen Pseudomonas aeruginosa PAO1 was determined to high resolution using the Se SAD method for initial phasing. The protein was found to be monomeric and the structure consists of two domains, domains 1 and 2, comprising residues 24 184 and 185 268, respectively. The fold of these domains could not be predicted even using state of the art prediction methods, and similarity searches revealed only a very distant homology to known structures, namely to Mog1p PsbP like and OmpA like proteins for the N and C terminal domains, respectively. Since PA1624 is only present in an important human pathogen, its unique structure and periplasmic location render it a potential drug target. Consequently, the results presented here may open new avenues for the discovery and design of antibacterial drugs |
| نوع الوثيقة: |
article in journal/newspaper |
| وصف الملف: |
application/pdf |
| اللغة: |
unknown |
| Relation: |
http://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=103201 |
| الاتاحة: |
http://www.helmholtz-berlin.de/pubbin/oai_publication?VT=1&ID=103201 |
| Rights: |
info:eu-repo/semantics/openAccess |
| رقم الانضمام: |
edsbas.BD22FABC |
| قاعدة البيانات: |
BASE |