2gl9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2gl9.gif|left|200px]]
{{Seed}}
[[Image:2gl9.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gl9|  PDB=2gl9  |  SCENE=  }}  
{{STRUCTURE_2gl9|  PDB=2gl9  |  SCENE=  }}  


'''Crystal Structure of Glycosylasparaginase-Substrate Complex'''
===Crystal Structure of Glycosylasparaginase-Substrate Complex===




==Overview==
<!--  
Glycosylasparaginase (GA) plays an important role in asparagine-linked glycoprotein degradation. A deficiency in the activity of human GA leads to a lysosomal storage disease named aspartylglycosaminuria. GA belongs to a superfamily of N-terminal nucleophile hydrolases that autoproteolytically generate their mature enzymes from inactive single chain protein precursors. The side-chain of the newly exposed N-terminal residue then acts as a nucleophile during substrate hydrolysis. By taking advantage of mutant enzyme of Flavobacterium meningosepticum GA with reduced enzymatic activity, we have obtained a crystallographic snapshot of a productive complex with its substrate (NAcGlc-Asn), at 2.0 A resolution. This complex structure provided us an excellent model for the Michaelis complex to examine the specific contacts critical for substrate binding and catalysis. Substrate binding induces a conformational change near the active site of GA. To initiate catalysis, the side-chain of the N-terminal Thr152 is polarized by the free alpha-amino group on the same residue, mediated by the side-chain hydroxyl group of Thr170. Cleavage of the amide bond is then accomplished by a nucleophilic attack at the carbonyl carbon of the amide linkage in the substrate, leading to the formation of an acyl-enzyme intermediate through a negatively charged tetrahedral transition state.
The line below this paragraph, {{ABSTRACT_PUBMED_17157318}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17157318 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17157318}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Oxyanion hole]]
[[Category: Oxyanion hole]]
[[Category: Proton-relay network]]
[[Category: Proton-relay network]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:13:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:18:44 2008''

Revision as of 16:18, 27 July 2008

File:2gl9.png

Template:STRUCTURE 2gl9

Crystal Structure of Glycosylasparaginase-Substrate Complex

Template:ABSTRACT PUBMED 17157318

About this Structure

2GL9 is a Protein complex structure of sequences from Elizabethkingia meningoseptica. Full crystallographic information is available from OCA.

Reference

Crystallographic snapshot of a productive glycosylasparaginase-substrate complex., Wang Y, Guo HC, J Mol Biol. 2007 Feb 9;366(1):82-92. Epub 2006 Sep 26. PMID:17157318

Page seeded by OCA on Sun Jul 27 19:18:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2gl9&oldid=662742"