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.


1t4d

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1t4d.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1t4d.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1t4d| PDB=1t4d | SCENE= }}
{{STRUCTURE_1t4d| PDB=1t4d | SCENE= }}
-
'''Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase (EcASADH), at 1.95 Angstrom resolution'''
+
===Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase (EcASADH), at 1.95 Angstrom resolution===
-
==Overview==
+
<!--
-
Two high-resolution structures have been determined for Eschericia coli aspartate beta-semialdehyde dehydrogenase (ecASADH), an enzyme of the aspartate biosynthetic pathway, which is a potential target for novel antimicrobial drugs. Both ASADH structures were of the open form and were refined to 1.95 A and 1.6 A resolution, allowing a more detailed comparison with the closed form of the enzyme than previously possible. A more complex scheme for domain closure is apparent with the subunit being split into two further sub-domains with relative motions about three hinge axes. Analysis of hinge data and torsion-angle difference plots is combined to allow the proposal of a detailed structural mechanism for ecASADH domain closure. Additionally, asymmetric distortions of individual subunits are identified, which form the basis for the previously reported "half-of-the-sites reactivity" (HOSR). A putative explanation of this arrangement is also presented, suggesting the HOSR system may provide a means for ecASADH to offset the energy required to remobilise flexible loops at the end of the reaction cycle, and hence avoid falling into an energy minimum.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15288787}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15288787 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15288787}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Hosr]]
[[Category: Hosr]]
[[Category: Lysine biosynthesis]]
[[Category: Lysine biosynthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:30:43 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:08:23 2008''

Revision as of 10:08, 27 July 2008

Image:1t4d.png

Template:STRUCTURE 1t4d

Crystal structure of Escherichia coli aspartate beta-semialdehyde dehydrogenase (EcASADH), at 1.95 Angstrom resolution

Template:ABSTRACT PUBMED 15288787

About this Structure

1T4D is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

High-resolution structures reveal details of domain closure and "half-of-sites-reactivity" in Escherichia coli aspartate beta-semialdehyde dehydrogenase., Nichols CE, Dhaliwal B, Lockyer M, Hawkins AR, Stammers DK, J Mol Biol. 2004 Aug 13;341(3):797-806. PMID:15288787

Page seeded by OCA on Sun Jul 27 13:08:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t4d"
Personal tools