4ald: Difference between revisions

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[[Image:4ald.gif|left|200px]]
[[Image:4ald.png|left|200px]]


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==Overview==
{{ABSTRACT_10048322}}
Fructose 1,6-bisphosphate aldolase catalyzes the reversible cleavage of fructose 1,6-bisphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde 3-phosphate or glyceraldehyde, respectively. Catalysis involves the formation of a Schiff's base intermediate formed at the epsilon-amino group of Lys229. The existing apo-enzyme structure was refined using the crystallographic free-R-factor and maximum likelihood methods that have been shown to give improved structural results that are less subject to model bias. Crystals were also soaked with the natural substrate (fructose 1,6-bisphosphate), and the crystal structure of this complex has been determined to 2.8 A. The apo structure differs from the previous Brookhaven-deposited structure (1ald) in the flexible C-terminal region. This is also the region where the native and complex structures exhibit differences. The conformational changes between native and complex structure are not large, but the observed complex does not involve the full formation of the Schiff's base intermediate, and suggests a preliminary hydrogen-bonded Michaelis complex before the formation of the covalent complex.


==About this Structure==
==About this Structure==
4ALD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 4ALD with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ALD OCA].  
4ALD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 4ALD with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ALD OCA].  
==Reference==
Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications., Dalby A, Dauter Z, Littlechild JA, Protein Sci. 1999 Feb;8(2):291-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10048322 10048322]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Fructose-bisphosphate aldolase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Tim barrel]]
[[Category: Tim barrel]]
[[Category: Type 1 aldolase]]
[[Category: Type 1 aldolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:20:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:28:26 2008''

Revision as of 15:28, 26 June 2008

File:4ald.png


Drag the structure with the mouse to rotate
4ald, resolution 2.80Å (default scene)
Ligands: 2FP
Activity: Fructose-bisphosphate aldolase, with EC number 4.1.2.13
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



HUMAN MUSCLE FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COMPLEXED WITH FRUCTOSE 1,6-BISPHOSPHATE


Template:ABSTRACT 10048322

About this Structure

4ALD is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 4ALD with [The Glycolytic Enzymes]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 18:28:26 2008

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