1DAW

CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-AMPPNP

Summary for 1DAW

• Entry DOI: 10.2210/pdb1daw/pdb
• Related: 1A6O 1DAY
• Descriptor: PROTEIN KINASE CK2, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• Functional Keywords: protein kinase ck2, dual-cosubstrate specificity, binary complex, transferase
• Biological source: Zea mays
• Total number of polymer chains: 1
• Total formula weight: 39228.20

Authors

Niefind, K.,Puetter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D. (deposition date: 1999-11-01, release date: 2000-05-03, Last modification date: 2023-08-09)

Primary citation

Niefind, K.,Putter, M.,Guerra, B.,Issinger, O.G.,Schomburg, D.
GTP plus water mimic ATP in the active site of protein kinase CK2.
Nat.Struct.Biol., 6:1100-1103, 1999

PubMed Abstract: The structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP were determined to 2.2 A resolution. Unlike most other protein kinases, CK2 from various sources shows 'dual-cosubstrate specificity', that is, the ability to efficiently use either ATP or GTP as a cosubstrate. The structures of these complexes demonstrate that water molecules are critical to switch the active site of CK2 from an ATP- to a GTP-compatible state. An understanding of the structural basis of dual-cosubstrate specificity may help in the design of drugs that target CK2 or other kinases with this property.

PubMed: 10581548
DOI: 10.1038/70033

Experimental method

X-RAY DIFFRACTION (2.2 Å)