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| | ==CRYSTAL STRUCTURE OF PEPTIDE-N(4)-(N-ACETYL-BETA-D-GLUCOSAMINYL) ASPARAGINE AMIDASE AT 2.2 ANGSTROMS RESOLUTION== | | ==CRYSTAL STRUCTURE OF PEPTIDE-N(4)-(N-ACETYL-BETA-D-GLUCOSAMINYL) ASPARAGINE AMIDASE AT 2.2 ANGSTROMS RESOLUTION== |
| - | <StructureSection load='1png' size='340' side='right' caption='[[1png]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='1png' size='340' side='right'caption='[[1png]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1png]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13253 Atcc 13253]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PNG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1png]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PNG FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1png OCA], [http://pdbe.org/1png PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1png RCSB], [http://www.ebi.ac.uk/pdbsum/1png PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1png FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1png OCA], [https://pdbe.org/1png PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1png RCSB], [https://www.ebi.ac.uk/pdbsum/1png PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1png ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PNGF_ELIMR PNGF_ELIMR]] Cleaves an entire glycan from a glycoprotein. Requires that the glycosylated asparagine moiety (reaction 1) be substituted on its amino (R1) and carboxyl (R2) terminus with a polypeptide chain. | + | [https://www.uniprot.org/uniprot/PNGF_ELIMR PNGF_ELIMR] Cleaves an entire glycan from a glycoprotein. Requires that the glycosylated asparagine moiety (reaction 1) be substituted on its amino (R1) and carboxyl (R2) terminus with a polypeptide chain. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 13253]] | + | [[Category: Elizabethkingia meningoseptica]] |
| - | [[Category: Kuhn, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Roey, P Van]] | + | [[Category: Kuhn P]] |
| - | [[Category: Hydrolase]] | + | [[Category: Van Roey P]] |
| Structural highlights
Function
PNGF_ELIMR Cleaves an entire glycan from a glycoprotein. Requires that the glycosylated asparagine moiety (reaction 1) be substituted on its amino (R1) and carboxyl (R2) terminus with a polypeptide chain.
Publication Abstract from PubMed
Peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F (PNGase F) is an amidase that cleaves the beta-aspartylglucosylamine bond of asparagine-linked glycans. The 34.8-kDa (314 amino acids) enzyme has a very broad substrate specificity and is extensively used for studies of the structure and function of glycoproteins. Enzymatic activity of PNGase F requires recognition of both the peptide and the carbohydrate components of the substrate. Only limited information regarding the mechanism of action of the enzyme is available. The three-dimensional structure of PNGase F has been determined by X-ray crystallography at 2.2-A resolution. The protein folds into two domains comprising residues 1-137 and 143-314, respectively. Both domains have eight-stranded antiparallel beta-sandwich motifs that are very similar in geometry. Both sandwiches have parallel principal axes and lie side by side. The covalent link between the domains is located at the top end of the molecule. Extensive hydrogen-bonding contacts occur along the full length of the interface between the two domains. Three different areas, all at the interface between the two domains, have been identified as possible locations for the active site of the enzyme. These include a hydrophobic bowl of about 20 A in diameter on one surface of the molecule, a long polar cleft on the opposite side, and a cleft at the bottom, which is lined with large aromatic residues including eight tryptophans.
Crystal structure of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F at 2.2-A resolution.,Kuhn P, Tarentino AL, Plummer TH Jr, Van Roey P Biochemistry. 1994 Oct 4;33(39):11699-706. PMID:7918386[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuhn P, Tarentino AL, Plummer TH Jr, Van Roey P. Crystal structure of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase F at 2.2-A resolution. Biochemistry. 1994 Oct 4;33(39):11699-706. PMID:7918386
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