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.


4fua

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:4fua.jpg|left|200px]]
[[Image:4fua.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 4fua |SIZE=350|CAPTION= <scene name='initialview01'>4fua</scene>, resolution 2.43&Aring;
+
The line below this paragraph, containing "STRUCTURE_4fua", creates the "Structure Box" on the page.
-
|SITE= <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion,+The+Four+Zn+...'>ACT</scene> and <scene name='pdbsite=PBS:Binding+Site+For+The+Substrate+Phosphate+Group'>PBS</scene>
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PGH:PHOSPHOGLYCOLOHYDROXAMIC+ACID'>PGH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_4fua| PDB=4fua | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fua OCA], [http://www.ebi.ac.uk/pdbsum/4fua PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4fua RCSB]</span>
+
-
}}
+
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH'''
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH'''
Line 28: Line 25:
[[Category: Dreyer, M K.]]
[[Category: Dreyer, M K.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
-
[[Category: class ii aldolase]]
+
[[Category: Class ii aldolase]]
-
[[Category: hydrolase]]
+
[[Category: Hydrolase]]
-
[[Category: zinc enzyme]]
+
[[Category: Zinc enzyme]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:24:03 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:46 2008''
+

Revision as of 19:24, 4 May 2008

Template:STRUCTURE 4fua

L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH


Overview

The structure of L-fuculose-1-phosphate aldolase in a cubic crystal form has been determined with and without the inhibitor phosphoglycolohydroxamate at 2.4 and 2.7 angstrom (1 angstrom = 0.1 nm) resolution, respectively. This inhibitor mimics the enediolate transition state of the substrate moiety dihydroxyacetone phosphate. The structures showed that dihydroxyacetone phosphate ligates the zinc ion of this metal-dependent class II aldolase with its hydroxyl and keto oxygen atoms, shifting Glu73 away from the zinc coordination sphere to a non-polar environment. At this position Glu73 accepts a proton in the initial reaction step, producing the enediolate which is then stabilized by the zinc ion. The other substrate moiety L-lactaldehyde was modeled, because no binding structure is yet available.

About this Structure

4FUA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Catalytic mechanism of the metal-dependent fuculose aldolase from Escherichia coli as derived from the structure., Dreyer MK, Schulz GE, J Mol Biol. 1996 Jun 14;259(3):458-66. PMID:8676381 Page seeded by OCA on Sun May 4 22:24:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools