Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.

K Niefind, B Guerra, L A Pinna, O G Issinger, D Schomburg

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

CK2alpha is the catalytic subunit of protein kinase CK2, an acidophilic and constitutively active eukaryotic Ser/Thr kinase involved in cell proliferation. A crystal structure, at 2.1 A resolution, of recombinant maize CK2alpha (rmCK2alpha) in the presence of ATP and Mg2+, shows the enzyme in an active conformation stabilized by interactions of the N-terminal region with the activation segment and with a cluster of basic residues known as the substrate recognition site. The close interaction between the N-terminal region and the activation segment is unique among known protein kinase structures and probably contributes to the constitutively active nature of CK2. The active centre is occupied by a partially disordered ATP molecule with the adenine base attached to a novel binding site of low specificity. This finding explains the observation that CK2, unlike other protein kinases, can use both ATP and GTP as phosphorylating agents.
Original languageEnglish
JournalEMBO Journal
Volume17
Issue number9
Pages (from-to)2451-62
Number of pages11
ISSN0261-4189
DOIs
Publication statusPublished - 1. May 1998

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Casein Kinase II
Zea mays
Catalytic Domain
Adenosine Triphosphate
Crystal structure
Protein Kinases
Chemical activation
Cell proliferation
Adenine
Guanosine Triphosphate
Conformations
Phosphotransferases
Binding Sites
Cell Proliferation
Molecules
Substrates
Enzymes

Keywords

  • Adenosine Triphosphate
  • Amino Acid Sequence
  • Binding Sites
  • Casein Kinase II
  • Crystallography, X-Ray
  • Guanosine Triphosphate
  • Macromolecular Substances
  • Magnesium
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein-Serine-Threonine Kinases
  • Recombinant Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Substrate Specificity
  • Zea mays

Cite this

@article{1664f04053db11ddb1a1000ea68e967b,
title = "Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.",
abstract = "CK2alpha is the catalytic subunit of protein kinase CK2, an acidophilic and constitutively active eukaryotic Ser/Thr kinase involved in cell proliferation. A crystal structure, at 2.1 A resolution, of recombinant maize CK2alpha (rmCK2alpha) in the presence of ATP and Mg2+, shows the enzyme in an active conformation stabilized by interactions of the N-terminal region with the activation segment and with a cluster of basic residues known as the substrate recognition site. The close interaction between the N-terminal region and the activation segment is unique among known protein kinase structures and probably contributes to the constitutively active nature of CK2. The active centre is occupied by a partially disordered ATP molecule with the adenine base attached to a novel binding site of low specificity. This finding explains the observation that CK2, unlike other protein kinases, can use both ATP and GTP as phosphorylating agents.",
keywords = "Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Casein Kinase II, Crystallography, X-Ray, Guanosine Triphosphate, Macromolecular Substances, Magnesium, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Protein-Serine-Threonine Kinases, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Substrate Specificity, Zea mays",
author = "K Niefind and B Guerra and Pinna, {L A} and Issinger, {O G} and D Schomburg",
year = "1998",
month = "5",
day = "1",
doi = "10.1093/emboj/17.9.2451",
language = "English",
volume = "17",
pages = "2451--62",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
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}

Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution. / Niefind, K; Guerra, B; Pinna, L A; Issinger, O G; Schomburg, D.

In: EMBO Journal, Vol. 17, No. 9, 01.05.1998, p. 2451-62.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution.

AU - Niefind, K

AU - Guerra, B

AU - Pinna, L A

AU - Issinger, O G

AU - Schomburg, D

PY - 1998/5/1

Y1 - 1998/5/1

N2 - CK2alpha is the catalytic subunit of protein kinase CK2, an acidophilic and constitutively active eukaryotic Ser/Thr kinase involved in cell proliferation. A crystal structure, at 2.1 A resolution, of recombinant maize CK2alpha (rmCK2alpha) in the presence of ATP and Mg2+, shows the enzyme in an active conformation stabilized by interactions of the N-terminal region with the activation segment and with a cluster of basic residues known as the substrate recognition site. The close interaction between the N-terminal region and the activation segment is unique among known protein kinase structures and probably contributes to the constitutively active nature of CK2. The active centre is occupied by a partially disordered ATP molecule with the adenine base attached to a novel binding site of low specificity. This finding explains the observation that CK2, unlike other protein kinases, can use both ATP and GTP as phosphorylating agents.

AB - CK2alpha is the catalytic subunit of protein kinase CK2, an acidophilic and constitutively active eukaryotic Ser/Thr kinase involved in cell proliferation. A crystal structure, at 2.1 A resolution, of recombinant maize CK2alpha (rmCK2alpha) in the presence of ATP and Mg2+, shows the enzyme in an active conformation stabilized by interactions of the N-terminal region with the activation segment and with a cluster of basic residues known as the substrate recognition site. The close interaction between the N-terminal region and the activation segment is unique among known protein kinase structures and probably contributes to the constitutively active nature of CK2. The active centre is occupied by a partially disordered ATP molecule with the adenine base attached to a novel binding site of low specificity. This finding explains the observation that CK2, unlike other protein kinases, can use both ATP and GTP as phosphorylating agents.

KW - Adenosine Triphosphate

KW - Amino Acid Sequence

KW - Binding Sites

KW - Casein Kinase II

KW - Crystallography, X-Ray

KW - Guanosine Triphosphate

KW - Macromolecular Substances

KW - Magnesium

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Protein Conformation

KW - Protein Structure, Secondary

KW - Protein-Serine-Threonine Kinases

KW - Recombinant Proteins

KW - Sequence Alignment

KW - Sequence Homology, Amino Acid

KW - Substrate Specificity

KW - Zea mays

U2 - 10.1093/emboj/17.9.2451

DO - 10.1093/emboj/17.9.2451

M3 - Journal article

VL - 17

SP - 2451

EP - 2462

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 9

ER -