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.

1j4b

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1j4b.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1j4b.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1j4b| PDB=1j4b | SCENE= }}
{{STRUCTURE_1j4b| PDB=1j4b | SCENE= }}
-
'''Recombinant Mouse-Muscle Adenylosuccinate Synthetase'''
+
===Recombinant Mouse-Muscle Adenylosuccinate Synthetase===
-
==Overview==
+
<!--
-
Vertebrates possess two isozymes of adenylosuccinate synthetase. The acidic isozyme is similar to the synthetase from bacteria and plants, being involved in the de novo biosynthesis of AMP, whereas the basic isozyme participates in the purine nucleotide cycle. Reported here is the first instance of overexpression and crystal structure determination of a basic isozyme of adenylosuccinate synthetase. The recombinant mouse muscle enzyme purified to homogeneity in milligram quantities exhibits a specific activity comparable with that of the rat muscle enzyme isolated from tissue and K(m) parameters for GTP, IMP, and l-aspartate (12, 45, and 140 microm, respectively) similar to those of the enzyme from Escherichia coli. The mouse muscle and E. coli enzymes have similar polypeptide folds, differing primarily in the conformation of loops, involved in substrate recognition and stabilization of the transition state. Residues 65-68 of the muscle isozyme adopt a conformation not observed in any previous synthetase structure. In its new conformation, segment 65-68 forms intramolecular hydrogen bonds with residues essential for the recognition of IMP and, in fact, sterically excludes IMP from the active site. Observed differences in ligand recognition among adenylosuccinate synthetases may be due in part to conformational variations in the IMP pocket of the ligand-free enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11560929}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11560929 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11560929}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Purine nucleotide cycle]]
[[Category: Purine nucleotide cycle]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:47:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:28:53 2008''

Revision as of 11:28, 1 July 2008

Image:1j4b.png

Template:STRUCTURE 1j4b

Recombinant Mouse-Muscle Adenylosuccinate Synthetase

Template:ABSTRACT PUBMED 11560929

About this Structure

1J4B is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Recombinant mouse muscle adenylosuccinate synthetase: overexpression, kinetics, and crystal structure., Iancu CV, Borza T, Choe JY, Fromm HJ, Honzatko RB, J Biol Chem. 2001 Nov 9;276(45):42146-52. Epub 2001 Sep 17. PMID:11560929

Page seeded by OCA on Tue Jul 1 14:28:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j4b"
Personal tools