We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1gvf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gvf.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1gvf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gvf| PDB=1gvf | SCENE= }}
{{STRUCTURE_1gvf| PDB=1gvf | SCENE= }}
-
'''STRUCTURE OF TAGATOSE-1,6-BISPHOSPHATE ALDOLASE'''
+
===STRUCTURE OF TAGATOSE-1,6-BISPHOSPHATE ALDOLASE===
-
==Overview==
+
<!--
-
Tagatose-1,6-bisphosphate aldolase (TBPA) is a tetrameric class II aldolase that catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate. The high resolution (1.45 A) crystal structure of the Escherichia coli enzyme, encoded by the agaY gene, complexed with phosphoglycolohydroxamate (PGH) has been determined. Two subunits comprise the asymmetric unit, and a crystallographic 2-fold axis generates the functional tetramer. A complex network of hydrogen bonds position side chains in the active site that is occupied by two cations. An unusual Na+ binding site is created using a pi interaction with Tyr183 in addition to five oxygen ligands. The catalytic Zn2+ is five-coordinate using three histidine nitrogens and two PGH oxygens. Comparisons of TBPA with the related fructose-1,6-bisphosphate aldolase (FBPA) identifies common features with implications for the mechanism. Because the major product of the condensation catalyzed by the enzymes differs in the chirality at a single position, models of FBPA and TBPA with their cognate bisphosphate products provide insight into chiral discrimination by these aldolases. The TBPA active site is more open on one side than FBPA, and this contributes to a less specific enzyme. The availability of more space and a wider range of aldehyde partners used by TBPA together with the highly specific nature of FBPA suggest that TBPA might be a preferred enzyme to modify for use in biotransformation chemistry.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11940603}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11940603 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11940603}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Zinc.]]
[[Category: Zinc.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:03:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:08:48 2008''

Revision as of 03:08, 1 July 2008

Image:1gvf.png

Template:STRUCTURE 1gvf

STRUCTURE OF TAGATOSE-1,6-BISPHOSPHATE ALDOLASE

Template:ABSTRACT PUBMED 11940603

About this Structure

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

Reference

Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases., Hall DR, Bond CS, Leonard GA, Watt CI, Berry A, Hunter WN, J Biol Chem. 2002 Jun 14;277(24):22018-24. Epub 2002 Apr 8. PMID:11940603

Page seeded by OCA on Tue Jul 1 06:08:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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