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[[Image:1pgs.gif|left|200px]]
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{{STRUCTURE_1pgs|  PDB=1pgs  |  SCENE=  }}
'''THE THREE-DIMENSIONAL STRUCTURE OF PNGASE F, A GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM'''


==THE THREE-DIMENSIONAL STRUCTURE OF PNGASE F, A GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM==
<StructureSection load='1pgs' size='340' side='right'caption='[[1pgs]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pgs]] 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=1PGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PGS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1pgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pgs OCA], [https://pdbe.org/1pgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pgs RCSB], [https://www.ebi.ac.uk/pdbsum/1pgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pgs ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== Publication Abstract from PubMed ==
BACKGROUND: Peptide:N-glycosidase F (PNGase F) is an enzyme that catalyzes the complete removal of N-linked oligosaccharide chains from glycoproteins. Often called an endoglycosidase, it is more correctly termed an amidase or glycosylasparaginase as cleavage is at the asparagine-sugar amide linkage. The enzyme is widely used in structure-function studies of glycoproteins. RESULTS: We have determined the crystal structure of PNGase F at 1.8 A resolution. The protein is folded into two domains, each with an eight-stranded antiparallel beta jelly roll configuration similar to many viral capsid proteins and also found, in expanded form, in lectins and several glucanases. Two potential active site regions have been identified, both in the interdomain region and shaped by prominent loops from one domain. Exposed aromatic residues are a feature of one site. CONCLUSIONS: The finding that PNGase F is based on two jelly roll domains suggests parallels with lectins and other carbohydrate-binding proteins. These proteins either bind sugars on the concave face of the beta-sandwich structure (aided by loops) or amongst the loops themselves. Further analysis of the function and identification of the catalytic site should lead to an understanding of both the specificity of PNGase F and possibly also the recognition processes that identify glycosylation sites on proteins.


==Overview==
The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum.,Norris GE, Stillman TJ, Anderson BF, Baker EN Structure. 1994 Nov 15;2(11):1049-59. PMID:7881905<ref>PMID:7881905</ref>
BACKGROUND: Peptide:N-glycosidase F (PNGase F) is an enzyme that catalyzes the complete removal of N-linked oligosaccharide chains from glycoproteins. Often called an endoglycosidase, it is more correctly termed an amidase or glycosylasparaginase as cleavage is at the asparagine-sugar amide linkage. The enzyme is widely used in structure-function studies of glycoproteins. RESULTS: We have determined the crystal structure of PNGase F at 1.8 A resolution. The protein is folded into two domains, each with an eight-stranded antiparallel beta jelly roll configuration similar to many viral capsid proteins and also found, in expanded form, in lectins and several glucanases. Two potential active site regions have been identified, both in the interdomain region and shaped by prominent loops from one domain. Exposed aromatic residues are a feature of one site. CONCLUSIONS: The finding that PNGase F is based on two jelly roll domains suggests parallels with lectins and other carbohydrate-binding proteins. These proteins either bind sugars on the concave face of the beta-sandwich structure (aided by loops) or amongst the loops themselves. Further analysis of the function and identification of the catalytic site should lead to an understanding of both the specificity of PNGase F and possibly also the recognition processes that identify glycosylation sites on proteins.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1PGS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PGS OCA].
</div>
<div class="pdbe-citations 1pgs" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The three-dimensional structure of PNGase F, a glycosylasparaginase from Flavobacterium meningosepticum., Norris GE, Stillman TJ, Anderson BF, Baker EN, Structure. 1994 Nov 15;2(11):1049-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7881905 7881905]
*[[Glycosylasparaginase|Glycosylasparaginase]]
*[[Peptide N-glycanase|Peptide N-glycanase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Anderson, B F.]]
[[Category: Anderson BF]]
[[Category: Baker, E N.]]
[[Category: Baker EN]]
[[Category: Norris, G E.]]
[[Category: Norris GE]]
[[Category: Stillman, T J.]]
[[Category: Stillman TJ]]
[[Category: Endoglycosidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:04:04 2008''

Latest revision as of 05:33, 5 June 2024

THE THREE-DIMENSIONAL STRUCTURE OF PNGASE F, A GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

1pgs, resolution 1.80Å

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