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PROSITE documentation PDOC51255ADP-dependent kinase (ADPK) domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51255
Although ATP is the most common phosphoryl group donor for kinases, certain hyperthermophilic archaea, such as Thermococcus litoralis and Pyrococcus furiosus, utilize unusual ADP-dependent glucokinases (ADPGKs) and phosphofructokinases (ADPPKKs) in their glycolytic pathways [1,2,3]. ADPGKs and ADPPFKs exhibit significant similarity, and form an ADP-dependent kinase (ADPK) family, which was tentatively named the PFKC family [4]. A ~460-residue ADPK domain is also found in a bifunctional ADP-dependent gluco/phosphofructo-kinase (ADP-GK/PFK) from Methanococcus jannaschii as well as in homologous hypothetical proteins present in several eukaryotes [5].
The whole structure of the ADPK domain can be divided into large and small α/β subdomains (see <PDB:1GC5; A>). The larger subdomain, which carries the ADP binding site, consists of a twisted 12-stranded β sheet flanked on both faces by 13 α helices and three 3(10) helices, forming an α/β 3-layer sandwich. The smaller subdomain, which covers the active site, forms an α/β two-layer structure containing 5 β strands and four α helices. The ADP molecule is buried in a shallow pocket in the large subdomain. The binding of substrate sugar induces a structural change, the small domain closing to form a complete substrate sugar binding site [1,2,3].
The profile we developed covers the entire ADPK domain.
Last update:October 2006 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Ito S. Fushinobu S. Yoshioka I. Koga S. Matsuzawa H. Wakagi T. |
| Title | Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon. | |
| Source | Structure 9:205-214(2001). | |
| PubMed ID | 11286887 |
| 2 | Authors | Tsuge H. Sakuraba H. Kobe T. Kujime A. Katunuma N. Ohshima T. |
| Title | Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-A resolution: a large conformational change in ADP-dependent glucokinase. | |
| Source | Protein Sci. 11:2456-2463(2002). | |
| PubMed ID | 12237466 |
| 3 | Authors | Ito S. Fushinobu S. Jeong J.-J. Yoshioka I. Koga S. Shoun H. Wakagi T. |
| Title | Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase. | |
| Source | J. Mol. Biol. 331:871-883(2003). | |
| PubMed ID | 12909015 |
| 4 | Authors | Ronimus R.S. Morgan H.W. |
| Title | The biochemical properties and phylogenies of phosphofructokinases from extremophiles. | |
| Source | Extremophiles 5:357-373(2001). | |
| PubMed ID | 11778837 |
| 5 | Authors | Verhees C.H. Tuininga J.E. Kengen S.W.M. Stams A.J.M. van der Oost J. de Vos W.M. |
| Title | ADP-dependent phosphofructokinases in mesophilic and thermophilic methanogenic archaea. | |
| Source | J. Bacteriol. 183:7145-7153(2001). | |
| PubMed ID | 11717273 | |
| DOI | 10.1128/JB.183.24.7145-7153.2001 |
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