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.


1p1x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p1x.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1p1x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p1x| PDB=1p1x | SCENE= }}
{{STRUCTURE_1p1x| PDB=1p1x | SCENE= }}
-
'''COMPARISON OF CLASS I ALDOLASE BINDING SITE ARCHITECTURE BASED ON THE CRYSTAL STRUCTURE OF 2-DEOXYRIBOSE-5-PHOSPHATE ALDOLASE DETERMINED AT 0.99 ANGSTROM RESOLUTION'''
+
===COMPARISON OF CLASS I ALDOLASE BINDING SITE ARCHITECTURE BASED ON THE CRYSTAL STRUCTURE OF 2-DEOXYRIBOSE-5-PHOSPHATE ALDOLASE DETERMINED AT 0.99 ANGSTROM RESOLUTION===
-
==Overview==
+
<!--
-
The crystal structure of the bacterial (Escherichia coli) class I 2-deoxyribose-5-phosphate aldolase (DERA) has been determined by Se-Met multiple anomalous dispersion (MAD) methods at 0.99A resolution. This structure represents the highest-resolution X-ray structure of an aldolase determined to date and enables a true atomic view of the enzyme. The crystal structure shows the ubiquitous TIM alpha/beta barrel fold. The enzyme contains two lysine residues in the active site. Lys167 forms the Schiff base intermediate, whereas Lys201, which is in close vicinity to the reactive lysine residue, is responsible for the perturbed pK(a) of Lys167 and, hence, also a key residue in the reaction mechanism. DERA is the only known aldolase that is able to use aldehydes as both aldol donor and acceptor molecules in the aldol reaction and is, therefore, of particular interest as a biocatalyst in synthetic organic chemistry. The uncomplexed DERA structure enables a detailed comparison with the substrate complexes and highlights a conformational change in the phosphate-binding site. Knowledge of the enzyme active-site environment has been the basis for exploration of catalysis of non-natural substrates and of mutagenesis of the phosphate-binding site to expand substrate specificity. Detailed comparison with other class I aldolase enzymes and DERA enzymes from different organisms reveals a similar geometric arrangement of key residues and implies a potential role for water as a general base in the catalytic mechanism.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15476818}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15476818 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15476818}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Alpha-beta barrel]]
[[Category: Alpha-beta barrel]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:34:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:44:18 2008''

Revision as of 23:44, 28 July 2008

Image:1p1x.png

Template:STRUCTURE 1p1x

COMPARISON OF CLASS I ALDOLASE BINDING SITE ARCHITECTURE BASED ON THE CRYSTAL STRUCTURE OF 2-DEOXYRIBOSE-5-PHOSPHATE ALDOLASE DETERMINED AT 0.99 ANGSTROM RESOLUTION

Template:ABSTRACT PUBMED 15476818

About this Structure

1P1X is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99A resolution., Heine A, Luz JG, Wong CH, Wilson IA, J Mol Biol. 2004 Oct 29;343(4):1019-34. PMID:15476818

Page seeded by OCA on Tue Jul 29 02:44:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p1x"
Personal tools