دورية أكاديمية
The crystal structure of rna1p: a new fold for a GTPase-activating protein.
| العنوان: | The crystal structure of rna1p: a new fold for a GTPase-activating protein. |
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| المؤلفون: | Hillig RC; Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Dortmund, Germany., Renault L, Vetter IR, Drell T 4th, Wittinghofer A, Becker J |
| المصدر: | Molecular cell [Mol Cell] 1999 Jun; Vol. 3 (6), pp. 781-91. |
| نوع المنشور: | Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Cell Press Country of Publication: United States NLM ID: 9802571 Publication Model: Print Cited Medium: Print ISSN: 1097-2765 (Print) Linking ISSN: 10972765 NLM ISO Abbreviation: Mol Cell Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Cambridge Ma : Cell Press Original Publication: Cambridge, Mass. : Cell Press, c1997- |
| مواضيع طبية MeSH: | GTP-Binding Proteins/*chemistry , GTP-Binding Proteins/*metabolism , Proteins/*chemistry , Proteins/*metabolism , Schizosaccharomyces/*chemistry, Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites ; Conserved Sequence ; Crystallography, X-Ray ; Fungal Proteins/chemistry ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; GTP-Binding Proteins/genetics ; GTPase-Activating Proteins ; Guanosine Triphosphate/metabolism ; Humans ; Hydrolysis ; Leucine/chemistry ; Leucine/genetics ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Proteins/genetics ; Schizosaccharomyces/genetics ; Schizosaccharomyces pombe Proteins ; ran GTP-Binding Protein ; ras GTPase-Activating Proteins |
| مستخلص: | rna1p is the Schizosaccharomyces pombe ortholog of the mammalian GTPase-activating protein (GAP) of Ran. Both proteins are essential for nuclear transport. Here, we report the crystal structure of rna1p at 2.66 A resolution. It contains 11 leucine-rich repeats that adopt the nonglobular shape of a crescent, bearing no resemblance to RhoGAP or RasGAP. The invariant residues of RanGAP form a contiguous surface, strongly indicating the Ran-binding interface. Alanine mutations identify Arg-74 as a critical residue for GTP hydrolysis. In contrast to RasGAP and RhoGAP, Arg-74 could be substituted by lysine and contributed significantly to the binding of Ran. Therefore, we suggest a GAP mechanism for rna1p, which constitutes a variation of the arginine finger mechanism found for Ras GAP and RhoGAP. |
| المشرفين على المادة: | 0 (Fungal Proteins) 0 (GTPase-Activating Proteins) 0 (Nuclear Proteins) 0 (Proteins) 0 (Schizosaccharomyces pombe Proteins) 0 (ras GTPase-Activating Proteins) 0 (rho GTPase-activating protein) 0 (rna1 protein, S pombe) 86-01-1 (Guanosine Triphosphate) EC 3.6.1.- (GTP-Binding Proteins) EC 3.6.5.2 (ran GTP-Binding Protein) GMW67QNF9C (Leucine) |
| تواريخ الأحداث: | Date Created: 19990708 Date Completed: 19990716 Latest Revision: 20190915 |
| رمز التحديث: | 20240627 |
| DOI: | 10.1016/s1097-2765(01)80010-1 |
| PMID: | 10394366 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1097-2765 |
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| DOI: | 10.1016/s1097-2765(01)80010-1 |