We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2gaw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2gaw.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2gaw.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2gaw| PDB=2gaw | SCENE= }}
{{STRUCTURE_2gaw| PDB=2gaw | SCENE= }}
-
'''WILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM'''
+
===WILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM===
-
==Overview==
+
<!--
-
Glycosylasparaginase (GA) is a member of a novel family of N-terminal nucleophile hydrolases that catalytically use an N-terminal residue as both a polarizing base and a nucleophile. These enzymes are activated from a single chain precursor by intramolecular autoproteolysis to yield the N-terminal nucleophile. A deficiency of GA results in the human genetic disorder known as aspartylglycosaminuria. In this study, we report the crystal structure of recombinant GA from Flavobacterium meningosepticum. Similar to the human structure, the bacterial GA forms an alphabetabetaalpha sandwich. However, some significant differences are observed between the Flavobacterium and human structures. The active site of Flavobacterium glycosylasparaginase is in an open conformation when compared with the human structure. We also describe the structure of a mutant wherein the N-terminal nucleophile Thr152 is substituted by a cysteine. In the bacterial GA crystals, we observe a heterotetrameric structure similar to that found in the human structure, as well as that observed in solution for eukaryotic glycosylasparaginases. The results confirm the suitability of the bacterial enzyme as a model to study the consequences of mutations in aspartylglycosaminuria patients. They also suggest that further studies are necessary to understand the detail mechanism of this enzyme. The presence of the heterotetrameric structure in the crystals is significant because dimerization of precursors has been suggested in the human enzyme to be a prerequisite to trigger autoproteolysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9685368}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9685368 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9685368}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Glycosylasparaginase]]
[[Category: Glycosylasparaginase]]
[[Category: N-terminal nucleophile hydrolase]]
[[Category: N-terminal nucleophile hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:53:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:28:50 2008''

Revision as of 08:28, 29 July 2008

Image:2gaw.png

Template:STRUCTURE 2gaw

WILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM

Template:ABSTRACT PUBMED 9685368

About this Structure

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

Reference

Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis., Guo HC, Xu Q, Buckley D, Guan C, J Biol Chem. 1998 Aug 7;273(32):20205-12. PMID:9685368

Page seeded by OCA on Tue Jul 29 11:28:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gaw"
Personal tools