4QAU

Crystal structure of F43Y mutant of sperm whale myoglobin

Summary for 4QAU

• Entry DOI: 10.2210/pdb4qau/pdb
• Related: 4IT8
• Descriptor: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: alpha helix boundle, oxygen transport, f43y mutant
• Biological source: Physeter catodon (Sperm whale)
• Total number of polymer chains: 1
• Total formula weight: 17998.64

Authors

Lin, Y.,Tan, X.,Li, W. (deposition date: 2014-05-06, release date: 2015-01-21, Last modification date: 2023-11-08)

Primary citation

Yan, D.-J.,Li, W.,Xiang, Y.,Wen, G.-B.,Lin, Y.-W.,Tan, X.
A Novel Tyrosine-Heme C-O Covalent Linkage in F43Y Myoglobin: A New Post-translational Modification of Heme Proteins
Chembiochem, 16:47-50, 2015

PubMed Abstract: Heme post-translational modification plays a key role in tuning the structure and function of heme proteins. We herein report a novel tyrosine-heme covalent C−O bond in an artificially produced sperm whale myoglobin (Mb) mutant, F43Y Mb, which formed spontaneously in vivo between the Tyr43 hydroxy group and the heme 4-vinyl group. This highlights the diverse chemistry of heme post-translational modifications, and lays groundwork for further investigation of the structural and functional diversity of covalently-bound heme proteins.

PubMed: 25392956
DOI: 10.1002/cbic.201402504

Experimental method

X-RAY DIFFRACTION (1.597 Å)