1a17

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[[Image:1a17.gif|left|200px]]<br /><applet load="1a17" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a17.gif|left|200px]]
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caption="1a17, resolution 2.45&Aring;" />
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'''TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5'''<br />
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{{Structure
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|PDB= 1a17 |SIZE=350|CAPTION= <scene name='initialview01'>1a17</scene>, resolution 2.45&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16]
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|GENE= PPP5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1A17 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A17 OCA].
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1A17 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A17 OCA].
==Reference==
==Reference==
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The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions., Das AK, Cohen PW, Barford D, EMBO J. 1998 Mar 2;17(5):1192-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9482716 9482716]
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The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions., Das AK, Cohen PW, Barford D, EMBO J. 1998 Mar 2;17(5):1192-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9482716 9482716]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Phosphoprotein phosphatase]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: phosphatase]]
[[Category: phosphatase]]
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[[Category: protein-protein interactions]]
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[[Category: protein-protein interaction]]
[[Category: super-helix]]
[[Category: super-helix]]
[[Category: tpr]]
[[Category: tpr]]
[[Category: x-ray structure]]
[[Category: x-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:51:22 2008''

Revision as of 07:51, 20 March 2008


PDB ID 1a17

Drag the structure with the mouse to rotate
, resolution 2.45Å
Ligands:
Gene: PPP5 (Homo sapiens)
Activity: Phosphoprotein phosphatase, with EC number 3.1.3.16
Coordinates: save as pdb, mmCIF, xml



TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5


Overview

The tetratricopeptide repeat (TPR) is a degenerate 34 amino acid sequence identified in a wide variety of proteins, present in tandem arrays of 3-16 motifs, which form scaffolds to mediate protein-protein interactions and often the assembly of multiprotein complexes. TPR-containing proteins include the anaphase promoting complex (APC) subunits cdc16, cdc23 and cdc27, the NADPH oxidase subunit p67 phox, hsp90-binding immunophilins, transcription factors, the PKR protein kinase inhibitor, and peroxisomal and mitochondrial import proteins. Here, we report the crystal structure of the TPR domain of a protein phosphatase, PP5. Each of the three TPR motifs of this domain consist of a pair of antiparallel alpha-helices of equivalent length. Adjacent TPR motifs are packed together in a parallel arrangement such that a tandem TPR motif structure is composed of a regular series of antiparallel alpha-helices. The uniform angular and spatial arrangement of neighbouring alpha-helices defines a helical structure and creates an amphipathic groove. Multiple-TPR motif proteins would fold into a right-handed super-helical structure with a continuous helical groove suitable for the recognition of target proteins, hence defining a novel mechanism for protein recognition. The spatial arrangement of alpha-helices in the PP5-TPR domain is similar to those within 14-3-3 proteins.

About this Structure

1A17 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions., Das AK, Cohen PW, Barford D, EMBO J. 1998 Mar 2;17(5):1192-9. PMID:9482716

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