Journal article
Crystal structure of a novel two domain GH78 family α-rhamnosidase from Klebsiella oxytoca with rhamnose bound
- Abstract:
- The crystal structure of the GH78 family α-rhamnosidase from Klebsiella oxytoca (KoRha) has been determined at 2.7 Å resolution with rhamnose bound in the active site of the catalytic domain. Curiously, the putative catalytic acid, Asp 222, is preceded by an unusual non-proline cis-peptide bond which helps to project the carboxyl group into the active centre. This KoRha homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays α-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Preview, Version of record, pdf, 535.2KB, Terms of use)
-
(Preview, Version of record, pdf, 1.2MB, Terms of use)
-
- Publisher copy:
- 10.1002/prot.24807
Authors
- Publisher:
- Wiley
- Journal:
- Proteins: Structure, Function, and Bioinformatics More from this journal
- Volume:
- 83
- Issue:
- 9
- Pages:
- 1742-1749
- Publication date:
- 2015-08-06
- Acceptance date:
- 2015-03-20
- DOI:
- ISSN:
-
0887-3585
- Keywords:
- Pubs id:
-
pubs:612908
- UUID:
-
uuid:a6674c83-e983-4f7f-a201-0b226001acba
- Local pid:
-
pubs:612908
- Source identifiers:
-
612908
- Deposit date:
-
2016-05-06
- ARK identifier:
Terms of use
- Copyright holder:
- Ellis O'Neill et al.
- Copyright date:
- 2015
- Notes:
- This is an open access article under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits use, distribution and reproduction in any medium,provided the original work is properly cited.
- Licence:
- CC Attribution (CC BY)
If you are the owner of this record, you can report an update to it here: Report update to this record