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.


1q2x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q2x.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1q2x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q2x| PDB=1q2x | SCENE= }}
{{STRUCTURE_1q2x| PDB=1q2x | SCENE= }}
-
'''Crystal Structure of the E243D Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae bound with substrate aspartate semialdehyde'''
+
===Crystal Structure of the E243D Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae bound with substrate aspartate semialdehyde===
-
==Overview==
+
<!--
-
The reversible dephosphorylation of beta-aspartyl phosphate to L-aspartate-beta-semialdehyde (ASA) in the aspartate biosynthetic pathway is catalyzed by aspartate-beta-semialdehyde dehydrogenase (ASADH). The product of this reaction is a key intermediate in the biosynthesis of diaminopimelic acid, an integral component of bacterial cell walls and a metabolic precursor of lysine and also a precursor in the biosynthesis of threonine, isoleucine and methionine. The structures of selected Haemophilus influenzae ASADH mutants were determined in order to evaluate the residues that are proposed to interact with the substrates ASA or phosphate. The substrate Km values are not altered by replacement of either an active-site arginine (Arg270) with a lysine or a putative phosphate-binding group (Lys246) with an arginine. However, the interaction of phosphate with the enzyme is adversely affected by replacement of Arg103 with lysine and is significantly altered when a neutral leucine is substituted at this position. A conservative Glu243 to aspartate mutant does not alter either ASA or phosphate binding, but instead results in an eightfold increase in the Km for the coenzyme NADP. Each of the mutations is shown to cause specific subtle active-site structural alterations and each of these changes results in decreases in catalytic efficiency ranging from significant (approximately 3% native activity) to substantial (&lt;0.1% native activity).
+
The line below this paragraph, {{ABSTRACT_PUBMED_15272161}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15272161 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15272161}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Enzyme]]
[[Category: Enzyme]]
[[Category: Tetrahedral intermediate]]
[[Category: Tetrahedral intermediate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:47:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:35:07 2008''

Revision as of 13:35, 28 July 2008

Image:1q2x.png

Template:STRUCTURE 1q2x

Crystal Structure of the E243D Mutant of Aspartate Semialdehyde Dehydrogenase from Haemophilus influenzae bound with substrate aspartate semialdehyde

Template:ABSTRACT PUBMED 15272161

About this Structure

1Q2X is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase., Blanco J, Moore RA, Faehnle CR, Coe DM, Viola RE, Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1388-95. Epub 2004, Jul 21. PMID:15272161

Page seeded by OCA on Mon Jul 28 16:35:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q2x"
Personal tools