1pgs: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1pgs.gif|left|200px]]
{{Seed}}
[[Image:1pgs.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pgs|  PDB=1pgs  |  SCENE=  }}  
{{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===




==Overview==
<!--  
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.
The line below this paragraph, {{ABSTRACT_PUBMED_7881905}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7881905 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7881905}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Stillman, T J.]]
[[Category: Stillman, T J.]]
[[Category: Endoglycosidase]]
[[Category: Endoglycosidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:04:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:03:07 2008''

Revision as of 10:03, 27 July 2008

File:1pgs.png

Template:STRUCTURE 1pgs

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

Template:ABSTRACT PUBMED 7881905

About this Structure

1PGS is a Single protein structure of sequence from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Sun Jul 27 13:03:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1pgs&oldid=647330"