1h0p: Difference between revisions
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'''CYCLOPHILIN_5 FROM C. ELEGANS''' | {{Structure | ||
|PDB= 1h0p |SIZE=350|CAPTION= <scene name='initialview01'>1h0p</scene>, resolution 1.75Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=DTT:2,3-DIHYDROXY-1,4-DITHIOBUTANE'>DTT</scene> | |||
|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= | |||
}} | |||
'''CYCLOPHILIN_5 FROM C. ELEGANS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1H0P is a [ | 1H0P 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=1H0P OCA]. | ||
==Reference== | ==Reference== | ||
Structural and biological characterisation of the gut-associated cyclophilin B isoforms from Caenorhabditis elegans., Picken NC, Eschenlauer S, Taylor P, Page AP, Walkinshaw MD, J Mol Biol. 2002 Sep 6;322(1):15-25. PMID:[http:// | Structural and biological characterisation of the gut-associated cyclophilin B isoforms from Caenorhabditis elegans., Picken NC, Eschenlauer S, Taylor P, Page AP, Walkinshaw MD, J Mol Biol. 2002 Sep 6;322(1):15-25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12215411 12215411] | ||
[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
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[[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 11:30:34 2008'' | ||
Revision as of 09:30, 20 March 2008
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| 1h0p, resolution 1.75Å | |||||||||||||
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| Ligands: | DTT | ||||||||||||
| Activity: | Peptidylprolyl isomerase, with EC number 5.2.1.8 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CYCLOPHILIN_5 FROM C. ELEGANS
Overview
The free-living nematode Caenorhabditis elegans expresses 18 cyclophilin isoforms, eight of which are conserved single domain forms, comprising two closely related secreted or type B forms (CYP-5 and CYP-6). Recombinant CYP-5 has been purified, crystallised and the X-ray structure solved to a resolution of 1.75A. The detailed molecular architecture most strongly resembles the structure of human cyclophilin B with conserved changes in loop structure and N and C-terminal extensions. Interestingly, the active site pocket is occupied by a molecule of dithiothreitol though this has little effect on the geometry of the active site which is similar to other cyclophilin structures. The peptidyl-prolyl isomerase activity of CYP-5 has been characterised against the substrate N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, and gives a k(cat)/K(m) value of 3.6x10(6)M(-1)s(-1) that compares with a value of 6.3x10(6)M(-1)s(-1) for human cyclophilin B. The immunosuppressive drug cyclosporin A binds and inhibits CYP-5 with an IC(50) value of 50nM, which is comparable to the value of 84nM found for human cyclophilin B. CYP-6 has 67% sequence identity with CYP-5 and a molecular model was built based on the CYP-5 crystal structure. The model shows that CYP-5 and CYP-6 are likely to have very similar structures, but with a markedly increased number of negative charges distributed around the surface of CYP-6. The spatial expression patterns of the cyclophilin B isoforms were examined using transgenic animals carrying a LacZ reporter fusion to these genes, and both cyp-5 and cyp-6 are found to be expressed in an overlapping fashion in the nematode gut. The temporal expression pattern of cyp-5 was further determined and revealed a constitutive expression pattern, with highest abundance levels being found in the embryo.
About this Structure
1H0P is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Structural and biological characterisation of the gut-associated cyclophilin B isoforms from Caenorhabditis elegans., Picken NC, Eschenlauer S, Taylor P, Page AP, Walkinshaw MD, J Mol Biol. 2002 Sep 6;322(1):15-25. PMID:12215411
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