| |
|
|
|
|
(2001) Montfort, Bart Augustinus van
The Escherichica coli mannitol permease or enzyme IImtl (Ellmtl) catalyses the uptake and concomitant phosphorylation of mannitol Ellmtl has a complex architecture with each subunit of the dimer consisting of three domains (A, B, and C). Protein and domain interactions are needed to transfer the phosphoryl group from the A to the B domain, but also to accomplish the actual phosphorylation of the carbohydrate by the B domain, while bound to the C domain. In addition, the energy for the translocation step catalyzed by the membrane-embedded C domain comes from a conformational coupling interaction between the C and a phosphorylated B domain. Identification of the B/C domain and dimer interface should, therefore, assist in the elucidation of the energy-coupling mechanism and the conformational interaction in Ellmtl. Unfortunately, high-resolution structures are not available for the B and C domain of Ellmtl. Thus a variety of other approaches must be employed to u!
nravel the details of these interactions. Some of them will be presented in this thesis.
zie: Summary.
Gebruik a.u.b. deze link om te verwijzen naar dit
document:
http://irs.ub.rug.nl/ppn/22032042X |
Meer informatie in de catalogus
Meer informatie in Picarta
![[print]](/images/ubprint.gif) Afdrukken op bestelling.
| ID |
27501 |
| Moeder ID |
27459 |
| Volgorde |
montfort.b.a.van. |
| Naam |
b.a.van.montfoort |
| Publiceren |
yes |
| Embargo t/m |
0000-01-01 |
| OAI-naam |
Dissertation |
| Path |
faculties/science/2001/b.a.van.montfoort/ |
| Naam Cover |
vp.gif |
| Gemodificeerd op: |
2013-02-15 14:28:01 |
| Digitaal ID |
43565cc9dd66f |
| Instelling |
Faculty of Mathematics and Natural Sciences |
| Plaats van uitgifte |
Groningen |
| Onderzoeksinstelling |
Choose your Research institute |
| Datum promotie |
2001-06-22 |
| Datum beschikbaarstelling |
2001-06-22 |
| Titel |
Identification of domain interfaces in the E. coli mannitol permease |
| Titelvolgorde |
identification of domain interfaces in the e. coli mannitol permease |
| Elektronisch |
yes |
| Ruilverkeer mogelijk |
no |
| Printen in opdracht |
yes |
| Exporteer? |
yes |
| Aantal pagina's |
150 |
| Publicatiejaar |
2001 |
| Verslagjaar |
2001 |
| Taal |
en |
| Type |
Dissertation |
| Samenvatting EN |
The Escherichica coli mannitol permease or enzyme IImtl (Ellmtl) catalyses the uptake and concomitant phosphorylation of mannitol Ellmtl has a complex architecture with each subunit of the dimer consisting of three domains (A, B, and C). Protein and domain interactions are needed to transfer the phosphoryl group from the A to the B domain, but also to accomplish the actual phosphorylation of the carbohydrate by the B domain, while bound to the C domain. In addition, the energy for the translocation step catalyzed by the membrane-embedded C domain comes from a conformational coupling interaction between the C and a phosphorylated B domain. Identification of the B/C domain and dimer interface should, therefore, assist in the elucidation of the energy-coupling mechanism and the conformational interaction in Ellmtl. Unfortunately, high-resolution structures are not available for the B and C domain of Ellmtl. Thus a variety of other approaches must be employed to u!
nravel the details of these interactions. Some of them will be presented in this thesis.
zie: Summary. |
| Uitgever |
University of Groningen |
| Relatie URI |
http://www.rug.nl/ |
| Rechten |
University of Groningen |
| PPN |
22032042X |
| ISBN |
90-367-1387-0; |
| Trefwoord GOO |
Fosfotransferase; Escherichia coli; Mannitol; Interfaces; Proefschriften (vorm); |
| Trefwoord NBC |
42.33; |
| Auteur |
Montfort, Bart Augustinus van; |
| Promotors |
Robillard, G.T.; Poolman, B.; |
|
|
| |
| To top
|
| |
© 2003-2007 RUG : De Rijksuniversiteit Groningen heeft de rechten van deze repository. Alle rechten voorbehouden. Powered by WildFire | |
