Crystal structure of human alpha-lactalbumin at 1.7 A resolution.
The three-dimensional X-ray structure of human alpha-lactalbumin, an important component of milk, has been determined at 1.7 A (0.17 nm) resolution by the method of molecular replacement, using the refined structure of baboon alpha-lactalbumin as the model structure. The two proteins are known to ha...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
1991
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| _version_ | 1797077519832186880 |
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| author | Acharya, K Ren, J Stuart, D Phillips, D Fenna, R |
| author_facet | Acharya, K Ren, J Stuart, D Phillips, D Fenna, R |
| author_sort | Acharya, K |
| collection | OXFORD |
| description | The three-dimensional X-ray structure of human alpha-lactalbumin, an important component of milk, has been determined at 1.7 A (0.17 nm) resolution by the method of molecular replacement, using the refined structure of baboon alpha-lactalbumin as the model structure. The two proteins are known to have more than 90% amino acid sequence identity and crystallize in the same orthorhombic space group, P2(1)2(1)2. The crystallographic refinement of the structure using the simulated annealing method, resulted in a crystallographic R-factor of 0.209 for the 11,373 observed reflections (F greater than or equal to 2 sigma (F)) between 8 and 1.7 A resolution. The model comprises 983 protein atoms, 90 solvent atoms and a bound calcium ion. In the final model, the root-mean-square deviations from ideality are 0.013 A for covalent bond distances and 2.9 degrees for bond angles. Superposition of the human and baboon alpha-lactalbumin structures yields a root-mean-square difference of 0.67 A for the 123 structurally equivalent C alpha atoms. The C terminus is flexible in the human alpha-lactalbumin molecule. The striking structural resemblance between alpha-lactalbumins and C-type lysozymes emphasizes the homologous evolutionary relationship between these two classes of proteins. |
| first_indexed | 2024-03-07T00:19:14Z |
| format | Journal article |
| id | oxford-uuid:7bf28849-d1c9-4214-936d-a6db0eee1250 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T00:19:14Z |
| publishDate | 1991 |
| record_format | dspace |
| spelling | oxford-uuid:7bf28849-d1c9-4214-936d-a6db0eee12502022-03-26T20:53:54ZCrystal structure of human alpha-lactalbumin at 1.7 A resolution.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:7bf28849-d1c9-4214-936d-a6db0eee1250EnglishSymplectic Elements at Oxford1991Acharya, KRen, JStuart, DPhillips, DFenna, RThe three-dimensional X-ray structure of human alpha-lactalbumin, an important component of milk, has been determined at 1.7 A (0.17 nm) resolution by the method of molecular replacement, using the refined structure of baboon alpha-lactalbumin as the model structure. The two proteins are known to have more than 90% amino acid sequence identity and crystallize in the same orthorhombic space group, P2(1)2(1)2. The crystallographic refinement of the structure using the simulated annealing method, resulted in a crystallographic R-factor of 0.209 for the 11,373 observed reflections (F greater than or equal to 2 sigma (F)) between 8 and 1.7 A resolution. The model comprises 983 protein atoms, 90 solvent atoms and a bound calcium ion. In the final model, the root-mean-square deviations from ideality are 0.013 A for covalent bond distances and 2.9 degrees for bond angles. Superposition of the human and baboon alpha-lactalbumin structures yields a root-mean-square difference of 0.67 A for the 123 structurally equivalent C alpha atoms. The C terminus is flexible in the human alpha-lactalbumin molecule. The striking structural resemblance between alpha-lactalbumins and C-type lysozymes emphasizes the homologous evolutionary relationship between these two classes of proteins. |
| spellingShingle | Acharya, K Ren, J Stuart, D Phillips, D Fenna, R Crystal structure of human alpha-lactalbumin at 1.7 A resolution. |
| title | Crystal structure of human alpha-lactalbumin at 1.7 A resolution. |
| title_full | Crystal structure of human alpha-lactalbumin at 1.7 A resolution. |
| title_fullStr | Crystal structure of human alpha-lactalbumin at 1.7 A resolution. |
| title_full_unstemmed | Crystal structure of human alpha-lactalbumin at 1.7 A resolution. |
| title_short | Crystal structure of human alpha-lactalbumin at 1.7 A resolution. |
| title_sort | crystal structure of human alpha lactalbumin at 1 7 a resolution |
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