4fua

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4fua.jpg|left|200px]]<br /><applet load="4fua" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:4fua.jpg|left|200px]]<br /><applet load="4fua" size="350" color="white" frame="true" align="right" spinBox="true"
caption="4fua, resolution 2.43&Aring;" />
caption="4fua, resolution 2.43&Aring;" />
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH'''<br />
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE COMPLEX WITH PGH'''<br />
Line 7: Line 7:
==About this Structure==
==About this Structure==
-
4FUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, SO4, BME and PGH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4FUA OCA].
+
4FUA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=BME:'>BME</scene> and <scene name='pdbligand=PGH:'>PGH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FUA OCA].
==Reference==
==Reference==
Line 24: Line 24:
[[Category: zinc enzyme]]
[[Category: zinc enzyme]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 20:44:02 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:52:53 2008''

Revision as of 08:52, 3 February 2008


4fua, resolution 2.43Å

Drag the structure with the mouse to rotate

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 with , , and as ligands. Active as L-fuculose-phosphate aldolase, with EC number 4.1.2.17 Known structural/functional Sites: and . 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 Feb 3 10:52:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools