| Autor: |
Junhyung Kim, Sojin Moon, Tod D. Romo, Yifei Yang, Euiyoung Bae, George N. Phillips Jr. |
| Jazyk: |
angličtina |
| Rok vydání: |
2024 |
| Předmět: |
|
| Zdroj: |
Structural Dynamics, Vol 11, Iss 1, Pp 014702-014702-12 (2024) |
| Druh dokumentu: |
article |
| ISSN: |
2329-7778 |
| DOI: |
10.1063/4.0000205 |
| Popis: |
Adenylate kinase is a ubiquitous enzyme in living systems and undergoes dramatic conformational changes during its catalytic cycle. For these reasons, it is widely studied by genetic, biochemical, and biophysical methods, both experimental and theoretical. We have determined the basic crystal structures of three differently liganded states of adenylate kinase from Methanotorrus igneus, a hyperthermophilic organism whose adenylate kinase is a homotrimeric oligomer. The multiple copies of each protomer in the asymmetric unit of the crystal provide a unique opportunity to study the variation in the structure and were further analyzed using advanced crystallographic refinement methods and analysis tools to reveal conformational heterogeneity and, thus, implied dynamic behaviors in the catalytic cycle. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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