| dc.contributor.author |
Christoforides, E |
en |
| dc.contributor.author |
Dimou, M |
en |
| dc.contributor.author |
Katinakis, P |
en |
| dc.contributor.author |
Bethanis, K |
en |
| dc.contributor.author |
Karpusas, M |
en |
| dc.date.accessioned |
2014-06-06T06:52:06Z |
|
| dc.date.available |
2014-06-06T06:52:06Z |
|
| dc.date.issued |
2012 |
en |
| dc.identifier.issn |
17443091 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1107/S1744309112000188 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5844 |
|
| dc.subject |
Azotobacter vinelandii |
en |
| dc.subject |
catalysis |
en |
| dc.subject |
isomerization |
en |
| dc.subject |
peptidyl-prolyl isomerases |
en |
| dc.subject.other |
cyclophilin A |
en |
| dc.subject.other |
peptide |
en |
| dc.subject.other |
amino acid sequence |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
chemical structure |
en |
| dc.subject.other |
chemistry |
en |
| dc.subject.other |
cytoplasm |
en |
| dc.subject.other |
enzymology |
en |
| dc.subject.other |
human |
en |
| dc.subject.other |
hydrogen bond |
en |
| dc.subject.other |
molecular genetics |
en |
| dc.subject.other |
protein domain |
en |
| dc.subject.other |
sequence alignment |
en |
| dc.subject.other |
Amino Acid Sequence |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
Cyclophilin A |
en |
| dc.subject.other |
Cytoplasm |
en |
| dc.subject.other |
Humans |
en |
| dc.subject.other |
Hydrogen Bonding |
en |
| dc.subject.other |
Models, Molecular |
en |
| dc.subject.other |
Molecular Sequence Data |
en |
| dc.subject.other |
Peptides |
en |
| dc.subject.other |
Protein Interaction Domains and Motifs |
en |
| dc.subject.other |
Sequence Alignment |
en |
| dc.subject.other |
Azotobacter vinelandii |
en |
| dc.subject.other |
Bacteria (microorganisms) |
en |
| dc.title |
Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1107/S1744309112000188 |
en |
| heal.publicationDate |
2012 |
en |
| heal.abstract |
Cyclophilins constitute a class of peptidyl-prolyl isomerases which participate in processes related to protein folding, signalling and chaperoning. The crystal structure of the cytoplasmic cyclophilin A (CyPA) from the bacterium Azotobacter vinelandii complexed with a synthetic tetrapeptide was determined by molecular replacement at 2 Å resolution. The proline in the tetrapeptide is observed to adopt the cis-isomer conformation. Comparisons of this structure with other CyPA structures provide insights into the conformational variability, effects of peptide binding and structure-function relationships of this enzyme. © 2012 International Union of Crystallography All rights reserved. |
en |
| heal.journalName |
Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
en |
| dc.identifier.issue |
3 |
en |
| dc.identifier.volume |
68 |
en |
| dc.identifier.doi |
10.1107/S1744309112000188 |
en |
| dc.identifier.spage |
259 |
en |
| dc.identifier.epage |
264 |
en |