5GZA

protein O-mannose kinase

Summary for 5GZA

• Entry DOI: 10.2210/pdb5gza/pdb
• Descriptor: Protein O-mannose kinase, 2-acetamido-2-deoxy-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-alpha-D-mannopyranose, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: protein o-mannose kinase, transferase
• Biological source: Danio rerio (Zebrafish)
• Cellular location: Endoplasmic reticulum membrane ; Single-pass type II membrane protein : Q5U3W1
• Total number of polymer chains: 1
• Total formula weight: 34179.00

Authors

Xiao, J. (deposition date: 2016-09-27, release date: 2016-12-07, Last modification date: 2024-11-06)

Primary citation

Zhu, Q.,Venzke, D.,Walimbe, A.S.,Anderson, M.E.,Fu, Q.,Kinch, L.N.,Wang, W.,Chen, X.,Grishin, N.V.,Huang, N.,Yu, L.,Dixon, J.E.,Campbell, K.P.,Xiao, J.
Structure of protein O-mannose kinase reveals a unique active site architecture
Elife, 5:-, 2016

PubMed Abstract: The 'pseudokinase' SgK196 is a protein O-mannose kinase (POMK) that catalyzes an essential phosphorylation step during biosynthesis of the laminin-binding glycan on α-dystroglycan. However, the catalytic mechanism underlying this activity remains elusive. Here we present the crystal structure of POMK in complex with Mg ions, ADP, aluminum fluoride, and the GalNAc-β3-GlcNAc-β4-Man trisaccharide substrate, thereby providing a snapshot of the catalytic transition state of this unusual kinase. The active site of POMK is established by residues located in non-canonical positions and is stabilized by a disulfide bridge. GalNAc-β3-GlcNAc-β4-Man is recognized by a surface groove, and the GalNAc-β3-GlcNAc moiety mediates the majority of interactions with POMK. Expression of various POMK mutants in knockout cells further validated the functional requirements of critical residues. Our results provide important insights into the ability of POMK to function specifically as a glycan kinase, and highlight the structural diversity of the human kinome.

PubMed: 27879205
DOI: 10.7554/eLife.22238

Experimental method

X-RAY DIFFRACTION (2 Å)