2at2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2at2.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2at2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2at2| PDB=2at2 | SCENE= }}
{{STRUCTURE_2at2| PDB=2at2 | SCENE= }}
-
'''MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION'''
+
===MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION===
-
==Overview==
+
<!--
-
The three-dimensional structure of Bacillus subtilis aspartate transcarbamoylase (ATCase; aspartate carbamoyltransferase; carbamoyl-phosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2) has been solved by the molecular replacement method at 3.0 A resolution and refined to a crystallographic R factor of 0.19. The enzyme crystallizes in the space group C2 with unit cell dimensions a = 258.5, b = 153.2, and c = 51.9 A and beta = 97.7 degrees. The asymmetric unit is composed of three monomers related by noncrystallographic threefold symmetry. A total of 295 of 304 amino acid residues have been built into the monomer. The last 9 residues in the C terminus were not included in the final model. Each monomer consists of 34% alpha-helix and 18% beta-strand. Three solvent-exposed loop regions (residues 69-84, 178-191, and 212-229) are not well defined in terms of electron density. The catalytic trimer of ATCase from B. subtilis shows great similarity to the catalytic trimer in Escherichia coli ATCase, which was used in constructing the model for molecular replacement. The unliganded trimer from B. subtilis, which is not cooperative, resembles the T (inactive) state slightly more than the R (active)-state form of the E. coli trimer. However, certain regions in the B. subtilis trimer exhibit shifts toward the E. coli R-state conformation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1906175}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1906175 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1906175}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Stevens, R C.]]
[[Category: Stevens, R C.]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:26:47 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:02:22 2008''

Revision as of 12:02, 29 July 2008

Image:2at2.png

Template:STRUCTURE 2at2

MOLECULAR STRUCTURE OF BACILLUS SUBTILIS ASPARTATE TRANSCARBAMOYLASE AT 3.0 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1906175

About this Structure

2AT2 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Molecular structure of Bacillus subtilis aspartate transcarbamoylase at 3.0 A resolution., Stevens RC, Reinisch KM, Lipscomb WN, Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6087-91. PMID:1906175

Page seeded by OCA on Tue Jul 29 15:02:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2at2"
Personal tools