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.


1r0m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1r0m.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1r0m.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1r0m| PDB=1r0m | SCENE= }}
{{STRUCTURE_1r0m| PDB=1r0m | SCENE= }}
-
'''Structure of Deinococcus radiodurans N-acylamino acid racemase at 1.3 : insights into a flexible binding pocket and evolution of enzymatic activity'''
+
===Structure of Deinococcus radiodurans N-acylamino acid racemase at 1.3 : insights into a flexible binding pocket and evolution of enzymatic activity===
-
==Overview==
+
<!--
-
N-acylamino acid racemase (NAAAR) catalyzes the racemization of N-acylamino acids and can be used in concert with an aminoacylase to produce enantiopure alpha-amino acids, a process that has potential industrial applications. Here we have cloned and characterized an NAAAR homologue from a radiation-resistant ancient bacterium, Deinococcus radiodurans. The expressed NAAAR racemized various substrates at an optimal temperature of 60 degrees C and had Km values of 24.8 mM and 12.3 mM for N-acetyl-D-methionine and N-acetyl-L-methionine, respectively. The crystal structure of NAAAR was solved to 1.3 A resolution using multiwavelength anomalous dispersion (MAD) methods. The structure consists of a homooctamer in which each subunit has an architecture characteristic of enolases with a capping domain and a (beta/alpha)7 beta barrel domain. The NAAAR.Mg2+ and NAAAR.N-acetyl-L-glutamine.Mg2+ structures were also determined, allowing us to define the Lys170-Asp195-Glu220-Asp245-Lys269 framework for catalyzing 1,1-proton exchange of N-acylamino acids. Four subsites enclosing the substrate are identified: catalytic site, metal-binding site, side-chain-binding region, and a flexible lid region. The high conservation of catalytic and metal-binding sites in different enolases reflects the essentiality of a common catalytic platform, allowing these enzymes to robustly abstract alpha-protons of various carboxylate substrates efficiently. The other subsites involved in substrate recognition are less conserved, suggesting that divergent evolution has led to functionally distinct enzymes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15313614}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15313614 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15313614}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Wu, C L.]]
[[Category: Wu, C L.]]
[[Category: Racemase]]
[[Category: Racemase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:55:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:37:01 2008''

Revision as of 08:37, 28 July 2008

Image:1r0m.png

Template:STRUCTURE 1r0m

Structure of Deinococcus radiodurans N-acylamino acid racemase at 1.3 : insights into a flexible binding pocket and evolution of enzymatic activity

Template:ABSTRACT PUBMED 15313614

About this Structure

1R0M is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.

Reference

Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans., Wang WC, Chiu WC, Hsu SK, Wu CL, Chen CY, Liu JS, Hsu WH, J Mol Biol. 2004 Sep 3;342(1):155-69. PMID:15313614

Page seeded by OCA on Mon Jul 28 11:37:01 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r0m"
Personal tools