@article{
 title = {A cis-proline in α-hemoglobin stabilizing protein directs the structural reorganization of α-hemoglobin},
 type = {article},
 year = {2009},
 pages = {29462-29469},
 volume = {284},
 id = {a280cdd1-9f7b-37f1-8e93-e668c33b7b99},
 created = {2023-01-10T01:45:27.256Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:45:27.256Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {α-Hemoglobin (αHb) stabilizing protein (AHSP) is expressed in erythropoietic tissues as an accessory factor in hemoglobin synthesis. AHSP forms a specific complex with αHb and suppresses the heme-catalyzed evolution of reactive oxygen species by converting αHb to a conformation in which the heme is coordinated at both axial positions by histidine side chains (bis-histidyl coordination). Currently, the detailed mechanism by which AHSP induces structural changes in αHb has not been determined. Here, we present x-ray crystallography, NMR spectroscopy, and mutagenesis data that identify, for the first time, the importance of an evolutionarily conserved proline, Pro30, in loop 1 of AHSP. Mutation of Pro30 to a variety of residue types results in reduced ability to convert αHb. In complex with-Hb, AHSP Pro30 adopts a cis-peptidyl conformation and makes contact with the N terminus of helix G in αHb. Mutations that stabilize the cis-peptidyl conformation of free AHSP, also enhance the αHb conversion activity. These findings suggest that AHSP loop 1 can transmit structural changes to the heme pocket of αHb, and, more generally, highlight the importance of cis-peptidyl prolyl residues in defining the conformation of regulatory protein loops. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.},
 bibtype = {article},
 author = {Gell, D.A. and Feng, L. and Zhou, S. and Jeffrey, P.D. and Bendak, K. and Gow, A. and Weiss, M.J. and Shi, Y. and Mackay, J.P.},
 doi = {10.1074/jbc.M109.027045},
 journal = {Journal of Biological Chemistry},
 number = {43}
}

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AHSP forms a specific complex with αHb and suppresses the heme-catalyzed evolution of reactive oxygen species by converting αHb to a conformation in which the heme is coordinated at both axial positions by histidine side chains (bis-histidyl coordination). Currently, the detailed mechanism by which AHSP induces structural changes in αHb has not been determined. Here, we present x-ray crystallography, NMR spectroscopy, and mutagenesis data that identify, for the first time, the importance of an evolutionarily conserved proline, Pro30, in loop 1 of AHSP. Mutation of Pro30 to a variety of residue types results in reduced ability to convert αHb. In complex with-Hb, AHSP Pro30 adopts a cis-peptidyl conformation and makes contact with the N terminus of helix G in αHb. Mutations that stabilize the cis-peptidyl conformation of free AHSP, also enhance the αHb conversion activity. These findings suggest that AHSP loop 1 can transmit structural changes to the heme pocket of αHb, and, more generally, highlight the importance of cis-peptidyl prolyl residues in defining the conformation of regulatory protein loops. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.","bibtype":"article","author":"Gell, D.A. and Feng, L. and Zhou, S. and Jeffrey, P.D. and Bendak, K. and Gow, A. and Weiss, M.J. and Shi, Y. and Mackay, J.P.","doi":"10.1074/jbc.M109.027045","journal":"Journal of Biological Chemistry","number":"43","bibtex":"@article{\n title = {A cis-proline in α-hemoglobin stabilizing protein directs the structural reorganization of α-hemoglobin},\n type = {article},\n year = {2009},\n pages = {29462-29469},\n volume = {284},\n id = {a280cdd1-9f7b-37f1-8e93-e668c33b7b99},\n created = {2023-01-10T01:45:27.256Z},\n file_attached = {false},\n profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},\n group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},\n last_modified = {2023-01-10T01:45:27.256Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n abstract = {α-Hemoglobin (αHb) stabilizing protein (AHSP) is expressed in erythropoietic tissues as an accessory factor in hemoglobin synthesis. AHSP forms a specific complex with αHb and suppresses the heme-catalyzed evolution of reactive oxygen species by converting αHb to a conformation in which the heme is coordinated at both axial positions by histidine side chains (bis-histidyl coordination). Currently, the detailed mechanism by which AHSP induces structural changes in αHb has not been determined. Here, we present x-ray crystallography, NMR spectroscopy, and mutagenesis data that identify, for the first time, the importance of an evolutionarily conserved proline, Pro30, in loop 1 of AHSP. Mutation of Pro30 to a variety of residue types results in reduced ability to convert αHb. In complex with-Hb, AHSP Pro30 adopts a cis-peptidyl conformation and makes contact with the N terminus of helix G in αHb. Mutations that stabilize the cis-peptidyl conformation of free AHSP, also enhance the αHb conversion activity. 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