دورية أكاديمية
Refined structures of oxidized flavodoxin from Anacystis nidulans.
| العنوان: | Refined structures of oxidized flavodoxin from Anacystis nidulans. |
|---|---|
| المؤلفون: | Drennan CL; Department of Biological Chemistry and Biophysics Research Division, University of Michigan, 930 N. University Ave., Ann Arbor, MI 48109, USA., Pattridge KA, Weber CH, Metzger AL, Hoover DM, Ludwig ML |
| المصدر: | Journal of molecular biology [J Mol Biol] 1999 Dec 03; Vol. 294 (3), pp. 711-24. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print Cited Medium: Print ISSN: 0022-2836 (Print) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: 1959- : London : Academic Press |
| مواضيع طبية MeSH: | Cyanobacteria/*chemistry , Flavodoxin/*chemistry, Amino Acid Sequence ; Binding Sites ; Crystallography, X-Ray ; Flavin Mononucleotide/metabolism ; Models, Molecular ; Molecular Sequence Data ; Oxidation-Reduction ; Peptides/chemistry ; Sequence Alignment ; Structure-Activity Relationship |
| مستخلص: | Flavodoxin from Anacystis nidulans (Synechococcus PCC 7942) was the first member of the flavodoxin family to be characterized, and is the structural prototype for the "long-chain" flavodoxins that have molecular masses of approximately 20 kDa. Crystal structure analyses and refinements of three orthorhombic forms of oxidized A. nidulans flavodoxin are reported, and salient features of the fold and the FMN binding site are compared with other flavodoxins. The structure of form I (wild-type: P212121, a=57.08 A, b=69.24 A, c=45.55 A), determined initially by multiple isomorphous replacement, has been refined to R=0.183 and R(free)=0.211 for data from 10.0 to 1.7 A resolution. Structures of form II (wild-type: P212121, a=60.05 A, b=65.85 A, c=51.36 A) and form III (Asn58Gly: P212121, a=51.30 A, b=59.15 A, c=94.44 A) have been determined by molecular replacement and refined versus data to 2.0 A and 1.85 A, respectively; the R values for forms II and III are 0.147 and 0.150. Changes in the molecular contacts that produce the alternative packings in these crystalline forms are analyzed. Deletion of the Asn side-chain in the mutant Asn58Gly removes an intermolecular stacking interaction and allows the alternative packing found in form III crystals. The functionally important 50's loop of the FMN binding site is less restrained by intermolecular contacts in these crystals but maintains the same conformation as in oxidized wild type protein. The structures reported here provide the starting point for structure-function studies of the reduced states and of mutants, described in the accompanying paper. (Copyright 1999 Academic Press.) |
| معلومات مُعتمدة: | GM 07315 United States GM NIGMS NIH HHS; GM 08270 United States GM NIGMS NIH HHS; GM 16429 United States GM NIGMS NIH HHS |
| سلسلة جزيئية: | PDB 1CZN; 1CZU; 1DO3 |
| المشرفين على المادة: | 0 (Flavodoxin) 0 (Peptides) 7N464URE7E (Flavin Mononucleotide) |
| تواريخ الأحداث: | Date Created: 19991228 Date Completed: 20000113 Latest Revision: 20131121 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1006/jmbi.1999.3151 |
| PMID: | 10610791 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0022-2836 |
|---|---|
| DOI: | 10.1006/jmbi.1999.3151 |