4BR0
rat NTPDase2 in complex with Ca AMPNP
Summary for 4BR0
| Entry DOI | 10.2210/pdb4br0/pdb |
| Related | 3CJ1 3CJ7 3CJ9 3CJA 4BQZ 4BR2 4BR4 4BR5 4BR7 4BR9 4BRA 4BRC 4BRD 4BRE 4BRF 4BRG 4BRH 4BRI 4BRK 4BRL 4BRM 4BRN 4BRO 4BRP 4BRQ |
| Descriptor | ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2, 5'-O-[(R)-hydroxy(phosphonoamino)phosphoryl]adenosine, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | hydrolase, apyrase, atpase, adpase, purinergic signalling, domain rotation, transition state, ntpdase |
| Biological source | RATTUS NORVEGICUS (NORWAY RAT) |
| Cellular location | Membrane; Multi-pass membrane protein (Potential): O35795 |
| Total number of polymer chains | 1 |
| Total formula weight | 51625.79 |
| Authors | Zebisch, M.,Schaefer, P.,Lauble, P.,Straeter, N. (deposition date: 2013-06-03, release date: 2013-07-17, Last modification date: 2024-10-23) |
| Primary citation | Zebisch, M.,Krauss, M.,Schaefer, P.,Lauble, P.,Straeter, N. Crystallographic Snapshots Along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases Structure, 21:1460-, 2013 Cited by PubMed Abstract: In vertebrates, membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) on the cell surface are responsible for signal conversion and termination in purinergic signaling by extracellular nucleotides. Here we present apo and complex structures of the rat NTPDase2 extracellular domain and Legionella pneumophila NTPDase1, including a high-resolution structure with a transition-state analog. Comparison of ATP and ADP binding modes shows how NTPDases engage the same catalytic site for hydrolysis of nucleoside triphosphates and diphosphates. We find that this dual specificity is achieved at the expense of base specificity. Structural and mutational studies indicate that a conserved active-site water is replaced by the phosphate product immediately after phosphoryl transfer. Partial base specificity for purines in LpNTPDase1 is based on a different intersubunit base binding site for pyrimidine bases. A comparison of the bacterial enzyme in six independent crystal forms shows that NTPDases can undergo a domain closure motion of at least 17°. PubMed: 23830739DOI: 10.1016/J.STR.2013.05.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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