Academic Journal
Cupredoxin-like domains in haemocyanins
| العنوان: | Cupredoxin-like domains in haemocyanins |
|---|---|
| المؤلفون: | Jaenicke, E., Büchler, K., Markl, J., Decker, H., Barends, T. |
| المصدر: | Biochemical Journal |
| سنة النشر: | 2010 |
| المجموعة: | Max Planck Society: MPG.PuRe |
| الوصف: | Haemocyanins are multimeric oxygen transport proteins, which bind oxygen to type 3 copper sites. Arthropod haemocyanins contain 75-kDa subunits, whereas molluscan haemocyanins contain 350-400-kDa subunits comprising seven or eight different 50 kDa FUs (functional units) designated FU-a to FU-h, each with an active site. FU-h possesses a tail of 100 amino acids not present in the other FUs. In the present study we show by X-ray crystallography that in FU-h of KLH1 (keyhole-limpet-haemocyanin isoform 1) the structure of the tail domain is cupredoxin-like but contains no copper. The copper-free domain 3 in arthropod haemocyanin subunits has also recently been reinterpreted as being cupredoxin-like. We propose that the cupredoxin-like domain in both haemocyanin types once served to upload copper to the active site of the oxygen-binding domain. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/urn/http://www.ncbi.nlm.nih.gov/pubmed/20025608; http://hdl.handle.net/11858/00-001M-0000-002C-5720-1; http://hdl.handle.net/11858/00-001M-0000-002C-5722-E |
| الاتاحة: | http://hdl.handle.net/11858/00-001M-0000-002C-5720-1 http://hdl.handle.net/11858/00-001M-0000-002C-5722-E |
| Rights: | info:eu-repo/semantics/restrictedAccess |
| رقم الانضمام: | edsbas.C38D6F99 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |