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.


1brm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1brm.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1brm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1brm| PDB=1brm | SCENE= }}
{{STRUCTURE_1brm| PDB=1brm | SCENE= }}
-
'''ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI'''
+
===ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI===
-
==Overview==
+
<!--
-
Aspartate beta-semialdehyde dehydrogenase (ASADH) lies at the first branch point in an essential aspartic biosynthetic pathway found in bacteria, fungi and the higher plants. Mutations in the asd gene encoding for ASADH that produce an inactive enzyme are lethal, which suggests that ASADH may be an effective target for antibacterial, herbicidal and fungicidal agents.We have solved the crystal structure of the Escherichia coli enzyme to 2.5 A resolution using single isomorphous replacement and 3-fold non-crystallographic symmetry. Each monomer has an N-terminal nucleotide-binding domain and a dimerisation domain. The presence of an essential cysteine locates the active site in a cleft between the two domains. The functional dimer has the appearance of a butterfly, with the NADP-binding domains forming the wings and the dimerisation domain forming the body.A histidine residue is identified as a likely acid/base catalyst in the enzymic reaction. Other amino acids implicated in the enzymic activity by mutagenesis are found in the active site region and define the substrate binding pocket.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10369777}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10369777 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10369777}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Nadp]]
[[Category: Nadp]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:52:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:36:52 2008''

Revision as of 16:36, 30 June 2008

Image:1brm.png

Template:STRUCTURE 1brm

ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 10369777

About this Structure

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

Reference

Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis., Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R, J Mol Biol. 1999 Jun 18;289(4):991-1002. PMID:10369777

Page seeded by OCA on Mon Jun 30 19:36:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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