¹H, ¹⁵N and ¹³C chemical shifts of the D. melanogaster myosin VI light chain androcam in high calcium.
Androcam is a calmodulin-like protein that acts as a testis-specific light chain to myosin VI during spermatogenesis in D. melanogaster. Modest, localized chemical shift changes that accompany Ca(2+) binding to the androcam N-terminal lobe indicate that unlike calmodulin, androcam does not undergo a dramatic conformational change upon binding calcium. Here we report the (1)H, (15)N and (13)C resonances of androcam in the high calcium (10 mM) state and show the extent of chemical shift changes for backbone resonances relative to the low calcium state.
Department of Biochemistry and Cell Biology, Rice University, Houston, TX 77254, USA.
Mehul K
MK
Joshi
Sean
S
Moran
Kevin R
KR
MacKenzie
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D029721:Drosophila Proteins / Q000737:chemistry*; D004331:Drosophila melanogaster / Q000378:metabolism*; D008969:Molecular Sequence Data; D018995:Myosin Heavy Chains / Q000737:chemistry*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D011522:Protons
C090181:Acam protein, Drosophila; D002135:Calcium-Binding Proteins; D002247:Carbon Isotopes; D029721:Drosophila Proteins; D009587:Nitrogen Isotopes; D011522:Protons; C089785:myosin VI; D018995:Myosin Heavy Chains; D002118:Calcium