Crystal Structures of Two Homologous Pathogenesisrelated Proteins from Yellow Lupine (Record no. 41413)
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| fixed length control field | 02127nam a2200205Ia 4500 |
| 003 - CONTROL NUMBER IDENTIFIER | |
| control field | MX-MdCICY |
| 005 - DATE AND TIME OF LATEST TRANSACTION | |
| control field | 20250625124654.0 |
| 040 ## - CATALOGING SOURCE | |
| Transcribing agency | CICY |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) | |
| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) | B-7080 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION | |
| fixed length control field | 250602s9999 xx |||||s2 |||| ||und|d |
| 245 10 - TITLE STATEMENT | |
| Title | Crystal Structures of Two Homologous Pathogenesisrelated Proteins from Yellow Lupine |
| 490 0# - SERIES STATEMENT | |
| Volume/sequential designation | Journal of Molecular Biology, 319(5), p.1223-1234, 2002 |
| 520 3# - SUMMARY, ETC. | |
| Summary, etc. | Pathogenesis-related class 10 (PR10)proteins are restricted to the plant kingdom where they are coded by multigene families and occur at high levels. In spite of their abundance, their physiological role is obscure although members of a distantly related subclass (cytokinin-specific binding proteins)are known to bind plant hormones. PR10 proteins are of special significance in legume plants where their expression patterns are related to infection by the symbiotic, nitrogen-fixing bacteria. Here we present the first crystal structures of classic PR10 proteins representing two homologues from one subclass in yellow lupine. The general fold is similar and, as in a birch pollen allergen, consists of a seven-stranded b-sheet wrapped around a long C-terminal helix. The mouth of a large pocket formed between the b-sheet and the helix seems a likely site for ligand binding. The shape of the pocket varies because, in variance with the rigid b-sheet, the helix shows unusual conformational variability consisting in bending, disorder, and axial shifting. A surface loop, proximal to the entrance to the internal cavity, shows an unusual structural conservation and rigidity in contrast to the high glycine content in its sequence. The loop is different from the so-called glycine-rich P-loops that bind phosphate groups of nucleotides, but it is very likely that it does play a role in ligand binding in PR10 proteins. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Biesiadka, J. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Bujacz, G. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Sikorski, M.M. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Jaskolski, M. |
| 856 40 - ELECTRONIC LOCATION AND ACCESS | |
| Uniform Resource Identifier | <a href="https://drive.google.com/file/d/14PumV0bboGGgzzxuMGQ_QOVCRJnJH1rf/view?usp=drivesdk">https://drive.google.com/file/d/14PumV0bboGGgzzxuMGQ_QOVCRJnJH1rf/view?usp=drivesdk</a> |
| Public note | Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) | |
| Source of classification or shelving scheme | Clasificación local |
| Koha item type | Documentos solicitados |
| Lost status | Source of classification or shelving scheme | Damaged status | Not for loan | Collection | Home library | Current library | Shelving location | Date acquired | Total checkouts | Full call number | Date last seen | Price effective from | Koha item type |
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| Clasificación local | Ref1 | CICY | CICY | Documento préstamo interbibliotecario | 25.06.2025 | B-7080 | 25.06.2025 | 25.06.2025 | Documentos solicitados |