4I94

Structure of BSK8 in complex with AMP-PNP

Summary for 4I94

• Entry DOI: 10.2210/pdb4i94/pdb
• Related: 4I93 4I94
• Descriptor: Probable serine/threonine-protein kinase At5g41260, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: protein kinase, pseudo kinase, cfg, alanine gatekeeper, transferase, brassinosteroid-signaling, amp-pnp, mg2+
• Biological source: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• Cellular location: Cell membrane; Lipid-anchor (Potential): Q9FHD7
• Total number of polymer chains: 2
• Total formula weight: 69837.38

Authors

Gruetter, C.,Rauh, D. (deposition date: 2012-12-04, release date: 2013-08-14, Last modification date: 2024-03-20)

Primary citation

Grutter, C.,Sreeramulu, S.,Sessa, G.,Rauh, D.
Structural Characterization of the RLCK Family Member BSK8: A Pseudokinase with an Unprecedented Architecture
J.Mol.Biol., 425:4455-4467, 2013

PubMed Abstract: Brassinosteroid signaling kinases (BSKs) are plant-specific receptor-like cytoplasmic protein kinases involved in the brassinosteroid signaling pathway. Unlike common protein kinases, they possess a naturally occurring alanine residue at the "gatekeeper" position, as well as other sequence variations. How BSKs activate downstream proteins such as BSU1, as well as the structural consequences of their unusual sequential features, was unclear. We crystallized the catalytic domain of BSK8 and solved its structure by multiple-wavelength anomalous dispersion phasing methods to a resolution of 1.5Å. In addition, a co-crystal structure of BSK8 with 5-adenylyl imidodiphosphate (AMP-PNP) revealed unusual conformational arrangements of the nucleotide phosphate groups and catalytic key motifs, typically not observed for active protein kinases. Sequential analysis and comparisons with known pseudokinase structures suggest that BSKs represent constitutively inactive protein kinases that regulate brassinosteroid signal transfer through an allosteric mechanism.

PubMed: 23911552
DOI: 10.1016/j.jmb.2013.07.034

Experimental method

X-RAY DIFFRACTION (1.8 Å)