2cst: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:2cst.gif|left|200px]]
{{Seed}}
[[Image:2cst.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2cst|  PDB=2cst  |  SCENE=  }}  
{{STRUCTURE_2cst|  PDB=2cst  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION'''
===CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION===




==Overview==
<!--
The crystal structure of chicken cytosolic aspartate aminotransferase (cAATase; EC 2.6.1.1) has been solved and refined at 1.9 A resolution. Orthorhombic crystals, space group P2(1)2(1)2(1), a = 56.4 A, b = 126.0 A and c = 142.3 A, were grown from polyethylene glycol solutions in the presence of maleate, a dicarboxylic inhibitor that forms a Michaelis-like complex. The pyridoxal form of the enzyme was used for crystallization. Diffraction data were collected using synchrotron radiation. The structure of the new orthorhombic crystal form was solved by molecular replacement using the partially refined 2.8 A resolution structure of the high-salt crystal form as a search model. The final value of the crystallographic R-factor after rigid body and restrained least-squares refinement is 0.175 with very good model geometry. The two 2-fold-related subunits of cAATase have distinct environments in the crystal lattice. Domain movement is strictly hindered by the lattice contacts in one subunit, while the second one possesses conformational freedom. Despite their different environments, both subunits were found in the closed conformation with one maleate molecule tightly bound in each active site. The present study allows a detailed comparison of the highly refined structures of the aspartate aminotransferase isozymes, and thus provide better insight into the role of conserved and variable residues in substrate recognition and catalysis.
The line below this paragraph, {{ABSTRACT_PUBMED_7897655}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7897655 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7897655}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Malashkevich, V N.]]
[[Category: Malashkevich, V N.]]
[[Category: Strokopytov, B V.]]
[[Category: Strokopytov, B V.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 22:58:15 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:58:14 2008''

Revision as of 05:58, 28 July 2008

File:2cst.png

Template:STRUCTURE 2cst

CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 7897655

About this Structure

2CST is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 A resolution., Malashkevich VN, Strokopytov BV, Borisov VV, Dauter Z, Wilson KS, Torchinsky YM, J Mol Biol. 1995 Mar 17;247(1):111-24. PMID:7897655

Page seeded by OCA on Mon Jul 28 08:58:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2cst&oldid=690980"