1dyw
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1dyw.gif|left|200px]] | + | [[Image:1dyw.gif|left|200px]] |
| - | + | ||
| - | '''BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A DIVERGENT LOOP CYCLOPHILIN FROM CAENORHABDITIS ELEGANS''' | + | {{Structure |
| + | |PDB= 1dyw |SIZE=350|CAPTION= <scene name='initialview01'>1dyw</scene>, resolution 1.80Å | ||
| + | |SITE= <scene name='pdbsite=CBS:Cyclosporin+Binding+Site'>CBS</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A DIVERGENT LOOP CYCLOPHILIN FROM CAENORHABDITIS ELEGANS''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1DYW is a [ | + | 1DYW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DYW OCA]. |
==Reference== | ==Reference== | ||
| - | Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans., Dornan J, Page AP, Taylor P, Wu S, Winter AD, Husi H, Walkinshaw MD, J Biol Chem. 1999 Dec 3;274(49):34877-83. PMID:[http:// | + | Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans., Dornan J, Page AP, Taylor P, Wu S, Winter AD, Husi H, Walkinshaw MD, J Biol Chem. 1999 Dec 3;274(49):34877-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10574961 10574961] |
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| Line 24: | Line 33: | ||
[[Category: rotamase]] | [[Category: rotamase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:46:42 2008'' |
Revision as of 08:46, 20 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A DIVERGENT LOOP CYCLOPHILIN FROM CAENORHABDITIS ELEGANS
Overview
Cyclophilin 3 (CYP-3) is one of the most abundantly expressed cyclophilin isoforms in the free living nematode Caenorhabditis elegans. The detailed post-embryonic expression pattern of the cyp-3 transcript is unusual, peaking during early larval development. The spatial expression pattern was examined via reporter gene analysis demonstrating that the cyp-3 transcript is exclusively expressed in the single anterior excretory cell. Recombinant cyclophilin 3 has been purified, crystallized and solved to a resolution of 1.8 A. The peptidyl-prolyl isomerase activity of CYP-3 has been characterized against the substrate N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, and gives a k(cat)/K(m) value of 2.4 x 10(6) M(-1) s(-1). The immunosuppressive drug cyclosporin A binds and inhibits CYP-3 with an IC(50) value of 16 nM, comparable with the range of values found for human cyclophilin A. The x-ray structure shows that the overall fold and active site geometry is similar to other cyclophilin structures. There are however a number of distinctive features, and we use this structure and amino acid sequence alignment analysis to identify a subgroup of "divergent-loop cyclophilins". This subgroup has a number of uniquely conserved features: an additional loop between residues 48 and 54 (KSGKPLH); two cysteine residues (Cys(40) and Cys(168)) that are in close proximity but remain in the unoxidized form, and two other conserved residues, His(54) and Glu(83). We suggest that these features are functionally important for the role played by this class of cyclophilins during cellular responses to stress caused by changes in the redox environment or by up-regulation of cellular activity. This study represents a detailed biological, biochemical, and structural characterization of a single cyclophilin isoform in the model organism Caenorhabditis elegans.
About this Structure
1DYW is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans., Dornan J, Page AP, Taylor P, Wu S, Winter AD, Husi H, Walkinshaw MD, J Biol Chem. 1999 Dec 3;274(49):34877-83. PMID:10574961
Page seeded by OCA on Thu Mar 20 10:46:42 2008
