1x3z
From Proteopedia
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| - | [[Image:1x3z.gif|left|200px]] | + | [[Image:1x3z.gif|left|200px]] |
| - | + | ||
| - | '''Structure of a peptide:N-glycanase-Rad23 complex''' | + | {{Structure |
| + | |PDB= 1x3z |SIZE=350|CAPTION= <scene name='initialview01'>1x3z</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SUC:SUCROSE'>SUC</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine_amidase Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.52 3.5.1.52] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of a peptide:N-glycanase-Rad23 complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1X3Z is a [ | + | 1X3Z is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X3Z OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins., Lee JH, Choi JM, Lee C, Yi KJ, Cho Y, Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9144-9. Epub 2005 Jun 17. PMID:[http:// | + | Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins., Lee JH, Choi JM, Lee C, Yi KJ, Cho Y, Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9144-9. Epub 2005 Jun 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15964983 15964983] |
[[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]] | [[Category: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein-protein-inhibitor complex]] | [[Category: protein-protein-inhibitor complex]] | ||
| - | ''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 15:04:51 2008'' |
Revision as of 13:04, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase, with EC number 3.5.1.52 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of a peptide:N-glycanase-Rad23 complex
Overview
In eukaryotes, misfolded proteins must be distinguished from correctly folded proteins during folding and transport processes by quality control systems. Yeast peptide:N-glycanase (yPNGase) specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists proteasome-mediated glycoprotein degradation by forming a complex with 26S proteasome through DNA repair protein, yRad23. Here, we describe the crystal structures of a yPNGase and XPC-binding domain of yRad23 (yRad23XBD, residues 238-309) complex and of a yPNGase-yRad23XBD complex bound to a caspase inhibitor, Z-VAD-fmk. yPNGase is formed with three domains, a core domain containing a Cys-His-Asp triad, a Zn-binding domain, and a Rad23-binding domain. Both N- and C-terminal helices of yPNGase interact with yRad23 through extensive hydrophobic interactions. The active site of yPNGase is located in a deep cleft that is formed with residues conserved in all PNGase members, and three sugar molecules are bound to this cleft. Complex structures in conjunction with mutational analyses revealed that the walls of the cleft block access to the active site of yPNGase by native glycoprotein, whereas the cleft is sufficiently wide to accommodate denatured glycoprotein, thus explaining the specificity of PNGase for denatured substrates.
About this Structure
1X3Z is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins., Lee JH, Choi JM, Lee C, Yi KJ, Cho Y, Proc Natl Acad Sci U S A. 2005 Jun 28;102(26):9144-9. Epub 2005 Jun 17. PMID:15964983
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