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.

1f1o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f1o.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1f1o.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f1o| PDB=1f1o | SCENE= }}
{{STRUCTURE_1f1o| PDB=1f1o | SCENE= }}
-
'''STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES'''
+
===STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES===
-
==Overview==
+
<!--
-
Adenylosuccinate lyase catalyzes two separate reactions in the de novo purine biosynthetic pathway. Through its dual action in this pathway, adenylosuccinate lyase plays an integral part in cellular replication and metabolism. Mutations in the human enzyme can result in severe neurological disorders, including mental retardation with autistic features. The crystal structure of adenylosuccinate lyase from the hyperthermophilic archaebacterium Pyrobaculum aerophilum has been determined to 2.1 A resolution. Although both the fold of the monomer and the architecture of the tetrameric assembly are similar to adenylosuccinate lyase from the thermophilic eubacterium Thermotoga maritima, the archaebacterial lyase contains unique features. Surprisingly, the structure of adenylosuccinate lyase from P. aerophilum reveals that this intracellular protein contains three disulfide bonds that contribute significantly to its stability against thermal and chemical denaturation. The observation of multiple disulfide bonds in the recombinant form of the enzyme suggests the need for further investigations into whether the intracellular environment of P. aerophilum, and possibly other hyperthermophiles, may be compatible with protein disulfide bond formation. In addition, the protein is shorter in P. aerophilum than it is in other organisms. This abbreviation results from an internal excision of a cluster of helices that may be involved in protein-protein interactions in other organisms and may relate to the observed clinical effects of human mutations in that region.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10926519}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10926519 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10926519}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Yeates, T.]]
[[Category: Yeates, T.]]
[[Category: Purine biosynthesis]]
[[Category: Purine biosynthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:46:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:20:41 2008''

Revision as of 23:20, 30 June 2008

Image:1f1o.png

Template:STRUCTURE 1f1o

STRUCTURAL STUDIES OF ADENYLOSUCCINATE LYASES

Template:ABSTRACT PUBMED 10926519

About this Structure

1F1O is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds., Toth EA, Worby C, Dixon JE, Goedken ER, Marqusee S, Yeates TO, J Mol Biol. 2000 Aug 11;301(2):433-50. PMID:10926519

Page seeded by OCA on Tue Jul 1 02:20:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f1o"
Personal tools