3I17

Crystal structure of the apo R132K:L121E mutant of cellular retinoic acid-binding protein II at 1.68 angstrom resolution

Summary for 3I17

• Entry DOI: 10.2210/pdb3i17/pdb
• Related: 2FS6 2FS7 3FA7
• Descriptor: Cellular retinoic acid-binding protein 2 (2 entities in total)
• Functional Keywords: crabpii, retinoic acid, retinoid, nucleus, retinol-binding, transport, vitamin a, lipid binding, retinal binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P29373
• Total number of polymer chains: 2
• Total formula weight: 31139.49

Authors

Jia, X.,Watson, C.T.,Geiger, J.H. (deposition date: 2009-06-25, release date: 2009-07-28, Last modification date: 2023-09-06)

Primary citation

Vasileiou, C.,Wang, W.,Jia, X.,Lee, K.S.,Watson, C.T.,Geiger, J.H.,Borhan, B.
Elucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff base.
Proteins, 77:812-822, 2009

PubMed Abstract: Cellular Retinoic Acid Binding Protein II (CRABPII) has been reengineered to specifically bind and react with all-trans-retinal to form a protonated Schiff base. Each step of this process has been dissected and four residues (Lys132, Tyr134, Arg111, and Glu121) within the CRABPII binding site have been identified as crucial for imine formation and/or protonation. The precise role of each residue has been examined through site directed mutagenesis and crystallographic studies. The crystal structure of the R132K:L121E-CRABPII (PDB-3I17) double mutant suggests a direct interaction between engineered Glu121 and the native Arg111, which is critical for both Schiff base formation and protonation.

PubMed: 19603486
DOI: 10.1002/prot.22495

Experimental method

X-RAY DIFFRACTION (1.68 Å)