Designing Sequence to Control Protein Function in an EF-Hand Protein
The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca2+ sensor versus signal modulator function. To understand how differences in amino acid sequence lead to differences in the response to Ca2+ binding, comparative analyses o...
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Published in | Journal of the American Chemical Society Vol. 126; no. 19; pp. 5990 - 5998 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Washington, DC
American Chemical Society
19.05.2004
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Abstract | The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca2+ sensor versus signal modulator function. To understand how differences in amino acid sequence lead to differences in the response to Ca2+ binding, comparative analyses of sequence and structures, combined with model building, were used to develop hypotheses about which amino acid residues control Ca2+-induced conformational changes. These results were used to generate a first design of calbindomodulin (CBM-1), a calbindin D9k re-engineered with 15 mutations to respond to Ca2+ binding with a conformational change similar to that of calmodulin. The gene for CBM-1 was synthesized, and the protein was expressed and purified. Remarkably, this protein did not exhibit any non-native-like molten globule properties despite the large number of mutations and the nonconservative nature of some of them. Ca2+-induced changes in CD intensity and in the binding of the hydrophobic probe, ANS, implied that CBM-1 does undergo Ca2+ sensorlike conformational changes. The X-ray crystal structure of Ca2+-CBM-1 determined at 1.44 Å resolution reveals the anticipated increase in hydrophobic surface area relative to the wild-type protein. A nascent calmodulin-like hydrophobic docking surface was also found, though it is occluded by the inter-EF-hand loop. The results from this first calbindomodulin design are discussed in terms of progress toward understanding the relationships between amino acid sequence, protein structure, and protein function for EF-hand CaBPs, as well as the additional mutations for the next CBM design. |
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AbstractList | The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca(2+) sensor versus signal modulator function. To understand how differences in amino acid sequence lead to differences in the response to Ca(2+) binding, comparative analyses of sequence and structures, combined with model building, were used to develop hypotheses about which amino acid residues control Ca(2+)-induced conformational changes. These results were used to generate a first design of calbindomodulin (CBM-1), a calbindin D(9k) re-engineered with 15 mutations to respond to Ca(2+) binding with a conformational change similar to that of calmodulin. The gene for CBM-1 was synthesized, and the protein was expressed and purified. Remarkably, this protein did not exhibit any non-native-like molten globule properties despite the large number of mutations and the nonconservative nature of some of them. Ca(2+)-induced changes in CD intensity and in the binding of the hydrophobic probe, ANS, implied that CBM-1 does undergo Ca(2+) sensorlike conformational changes. The X-ray crystal structure of Ca(2+)-CBM-1 determined at 1.44 A resolution reveals the anticipated increase in hydrophobic surface area relative to the wild-type protein. A nascent calmodulin-like hydrophobic docking surface was also found, though it is occluded by the inter-EF-hand loop. The results from this first calbindomodulin design are discussed in terms of progress toward understanding the relationships between amino acid sequence, protein structure, and protein function for EF-hand CaBPs, as well as the additional mutations for the next CBM design. The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca2+ sensor versus signal modulator function. To understand how differences in amino acid sequence lead to differences in the response to Ca2+ binding, comparative analyses of sequence and structures, combined with model building, were used to develop hypotheses about which amino acid residues control Ca2+-induced conformational changes. These results were used to generate a first design of calbindomodulin (CBM-1), a calbindin D9k re-engineered with 15 mutations to respond to Ca2+ binding with a conformational change similar to that of calmodulin. The gene for CBM-1 was synthesized, and the protein was expressed and purified. Remarkably, this protein did not exhibit any non-native-like molten globule properties despite the large number of mutations and the nonconservative nature of some of them. Ca2+-induced changes in CD intensity and in the binding of the hydrophobic probe, ANS, implied that CBM-1 does undergo Ca2+ sensorlike conformational changes. The X-ray crystal structure of Ca2+-CBM-1 determined at 1.44 Å resolution reveals the anticipated increase in hydrophobic surface area relative to the wild-type protein. A nascent calmodulin-like hydrophobic docking surface was also found, though it is occluded by the inter-EF-hand loop. The results from this first calbindomodulin design are discussed in terms of progress toward understanding the relationships between amino acid sequence, protein structure, and protein function for EF-hand CaBPs, as well as the additional mutations for the next CBM design. |
Author | Mizoue, Laura S Bunick, Gerard J Hunter, Michael J Nelson, Melanie R Chazin, Walter J Bunick, Christopher G Mangahas, Sheryll Sheehan, Jonathan H |
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Keywords | Helix loop helix structure Binding protein Calbindin Biochemical analysis Secondary structure Conformational changes Calmodulin Fluorescence spectrometry Aminoacid sequence Structural analysis |
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Snippet | The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca2+ sensor versus signal... The extent of conformational change that calcium binding induces in EF-hand proteins is a key biochemical property specifying Ca(2+) sensor versus signal... |
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SubjectTerms | Amino Acid Sequence Amino Acids - chemistry Analytical, structural and metabolic biochemistry Binding and carrier proteins Biological and medical sciences Calbindins Calcium Signaling - physiology Calmodulin - chemistry Calmodulin - genetics Crystallography, X-Ray Drug Design EF Hand Motifs - genetics Fundamental and applied biological sciences. Psychology Models, Molecular Molecular Sequence Data Mutation - genetics Protein Conformation Proteins S100 Calcium Binding Protein G - chemistry S100 Calcium Binding Protein G - genetics Structure-Activity Relationship |
Title | Designing Sequence to Control Protein Function in an EF-Hand Protein |
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