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.


1rcq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rcq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rcq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rcq| PDB=1rcq | SCENE= }}
{{STRUCTURE_1rcq| PDB=1rcq | SCENE= }}
-
'''The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms'''
+
===The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms===
-
==Overview==
+
<!--
-
The structure of the catabolic alanine racemase, DadX, from the pathogenic bacterium Pseudomonas aeruginosa, reported here at 1.45 A resolution, is a dimer in which each monomer is comprised of two domains, an eight-stranded alpha/beta barrel containing the PLP cofactor and a second domain primarily composed of beta-strands. The geometry of each domain is very similar to that of Bacillus stearothermophilus alanine racemase, but the rotation between domains differs by about 15 degrees. This change does not alter the structure of the active site in which almost all residues superimpose well with a low rms difference of 0.86 A. Unexpectedly, the active site of DadX contains a guest substrate that is located where acetate and propionate have been observed in the Bacillus structures. It is modeled as d-lysine and oriented such that its terminal NZ atom makes a covalent bond with C4' of PLP. Since the internal aldimine bond between the protein lysine, Lys33, and C4' of PLP is also unambiguously observed, there appears to be an equilibrium between both internally and externally reacted forms. The PLP cofactor adopts two partially occupied conformational states that resemble previously reported internal and external aldimine complexes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14674749}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14674749 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14674749}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Beta-structure for c-terminal domain]]
[[Category: Beta-structure for c-terminal domain]]
[[Category: Internal/external aldimine form]]
[[Category: Internal/external aldimine form]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:20:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:02:59 2008''

Revision as of 17:03, 28 July 2008

Image:1rcq.png

Template:STRUCTURE 1rcq

The 1.45 A crystal structure of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms

Template:ABSTRACT PUBMED 14674749

About this Structure

1RCQ is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

Reference

Crystal structure at 1.45 A resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms., LeMagueres P, Im H, Dvorak A, Strych U, Benedik M, Krause KL, Biochemistry. 2003 Dec 23;42(50):14752-61. PMID:14674749

Page seeded by OCA on Mon Jul 28 20:02:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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