4BGA
Nucleotide-bound open form of a putative sugar kinase MK0840 from Methanopyrus kandleri
Summary for 4BGA
| Entry DOI | 10.2210/pdb4bga/pdb |
| Related | 4BG8 4BG9 4BGB |
| Related PRD ID | PRD_900003 |
| Descriptor | PREDICTED MOLECULAR CHAPERONE DISTANTLY RELATED TO HSP70-F OLD METALLOPROTEASES, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, POTASSIUM ION, ... (7 entities in total) |
| Functional Keywords | transferase, askha superfamily, phosphotransfer, pseudomurein |
| Biological source | METHANOPYRUS KANDLERI |
| Total number of polymer chains | 4 |
| Total formula weight | 143738.35 |
| Authors | Schacherl, M.,Baumann, U. (deposition date: 2013-03-24, release date: 2013-11-27, Last modification date: 2023-12-20) |
| Primary citation | Schacherl, M.,Waltersperger, S.M.,Baumann, U. Structural Characterization of the Ribonuclease H-Like Type Askha Superfamily Kinase Mk0840 from Methanopyrus Kandleri Acta Crystallogr.,Sect.D, 69:2440-, 2013 Cited by PubMed Abstract: Murein recycling is a process in which microorganisms recover peptidoglycan-degradation products in order to utilize them in cell wall biosynthesis or basic metabolic pathways. Methanogens such as Methanopyrus kandleri contain pseudomurein, which differs from bacterial murein in its composition and branching. Here, four crystal structures of the putative sugar kinase MK0840 from M. kandleri in apo and nucleotide-bound states are reported. MK0840 shows high similarity to bacterial anhydro-N-acetylmuramic acid kinase, which is involved in murein recycling. The structure shares a common fold with panthothenate kinase and the 2-hydroxyglutaryl-CoA dehydratase component A, both of which are members of the ASKHA (acetate and sugar kinases/Hsc70/actin) superfamily of phosphotransferases. Local conformational changes in the nucleotide-binding site between the apo and holo forms are observed upon nucleotide binding. Further insight is given into domain movements and putative active-site residues are identified. PubMed: 24311585DOI: 10.1107/S0907444913022683 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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