This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1j20

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1j20.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1j20.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1j20| PDB=1j20 | SCENE= }}
{{STRUCTURE_1j20| PDB=1j20 | SCENE= }}
-
'''Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with product'''
+
===Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with product===
-
==Overview==
+
<!--
-
Argininosuccinate synthetase reversibly catalyzes the ATP-dependent condensation of a citrulline with an aspartate to give argininosuccinate. The structures of the enzyme from Thermus thermophilus HB8 complexed with intact ATP and substrates (citrulline and aspartate) and with AMP and product (argininosuccinate) have been determined at 2.1- and 2.0-A resolution, respectively. The enzyme does not show the ATP-induced domain rotation observed in the enzyme from Escherichia coli. In the enzyme-substrate complex, the reaction sites of ATP and the bound substrates are adjacent and are sufficiently close for the reaction to proceed without the large conformational change at the domain level. The mobility of the triphosphate group in ATP and the side chain of citrulline play an important role in the catalytic action. The protonated amino group of the bound aspartate interacts with the alpha-phosphate of ATP and the ureido group of citrulline, thus stimulating the adenylation of citrulline. The enzyme-product complex explains how the citrullyl-AMP intermediate is bound to the active site. The stereochemistry of the catalysis of the enzyme is clarified on the basis of the structures of tAsS (argininosuccinate synthetase from T. thermophilus HB8) complexes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12684518}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12684518 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12684518}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:42:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:23:03 2008''

Revision as of 11:23, 1 July 2008

Image:1j20.png

Template:STRUCTURE 1j20

Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with product

Template:ABSTRACT PUBMED 12684518

About this Structure

1J20 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structures of argininosuccinate synthetase in enzyme-ATP substrates and enzyme-AMP product forms: stereochemistry of the catalytic reaction., Goto M, Omi R, Miyahara I, Sugahara M, Hirotsu K, J Biol Chem. 2003 Jun 20;278(25):22964-71. Epub 2003 Apr 8. PMID:12684518

Page seeded by OCA on Tue Jul 1 14:23:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j20"
Personal tools