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.


4gsa

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4gsa.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:4gsa.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4gsa| PDB=4gsa | SCENE= }}
{{STRUCTURE_4gsa| PDB=4gsa | SCENE= }}
-
'''CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE'''
+
===CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE===
-
==Overview==
+
<!--
-
The three-dimensional structure of glutamate-1-semialdehyde aminomutase (EC 5.4.3.8), an alpha2-dimeric enzyme from Synechococcus, has been determined by x-ray crystallography using heavy atom derivative phasing. The structure, refined at 2.4-A resolution to an R-factor of 18.7% and good stereochemistry, explains many of the enzyme's unusual specificity and functional properties. The overall fold is that of aspartate aminotransferase and related B6 enzymes, but it also has specific features. The structure of the complex with gabaculine, a substrate analogue, shows unexpectedly that the substrate binding site involves residues from the N-terminal domain of the molecule, notably Arg-32. Glu-406 is suitably positioned to repel alpha-carboxylic acids, thereby suggesting a basis for the enzyme's reaction specificity. The subunits show asymmetry in cofactor binding and in the mobilities of the residues 153-181. In the unliganded enzyme, one subunit has the cofactor bound as an aldimine of pyridoxal phosphate with Lys-273 and, in this subunit, residues 153-181 are disordered. In the other subunit in which the cofactor is not covalently bound, residues 153-181 are well defined. Consistent with the crystallographically demonstrated asymmetry, a form of the enzyme in which both subunits have pyridoxal phosphate bound to Lys-273 through a Schiff base showed biphasic reduction by borohydride in solution. Analysis of absorption spectra during reduction provided evidence of communication between the subunits. The crystal structure of the reduced form of the enzyme shows that, despite identical cofactor binding in each monomer, the structural asymmetry at residues 153-181 remains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9144156}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9144156 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9144156}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Pyridoxamine-5'-phosphate]]
[[Category: Pyridoxamine-5'-phosphate]]
[[Category: Reduced form]]
[[Category: Reduced form]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:24:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:39:25 2008''

Revision as of 10:39, 3 July 2008

Image:4gsa.png

Template:STRUCTURE 4gsa

CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE

Template:ABSTRACT PUBMED 9144156

About this Structure

4GSA is a Single protein structure of sequence from Synechococcus sp.. Full crystallographic information is available from OCA.

Reference

Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity., Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN, Proc Natl Acad Sci U S A. 1997 May 13;94(10):4866-71. PMID:9144156

Page seeded by OCA on Thu Jul 3 13:39:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gsa"
Personal tools