1fua: Difference between revisions

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[[Image:1fua.gif|left|200px]]<br /><applet load="1fua" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1fua.gif|left|200px]]
caption="1fua, resolution 1.92&Aring;" />
 
'''L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T'''<br />
{{Structure
|PDB= 1fua |SIZE=350|CAPTION= <scene name='initialview01'>1fua</scene>, resolution 1.92&Aring;
|SITE= <scene name='pdbsite=ACT:The+Active+Center+Is+Defined+By+The+Zn+Ion+And+The+Four+...'>ACT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene>
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1FUA 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> and <scene name='pdbligand=BME:'>BME</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+And+The+Four+...'>ACT</scene> and <scene name='pdbsite=PBS:The+Substrate+Phosphate+Binding+Site+Near+The+Active+Cen+...'>PBS</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUA OCA].  
1FUA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUA OCA].  


==Reference==
==Reference==
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli., Dreyer MK, Schulz GE, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299567 15299567]
Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli., Dreyer MK, Schulz GE, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299567 15299567]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: L-fuculose-phosphate aldolase]]
[[Category: L-fuculose-phosphate aldolase]]
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[[Category: zinc enzyme]]
[[Category: zinc enzyme]]


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Revision as of 12:14, 20 March 2008

File:1fua.gif


PDB ID 1fua

Drag the structure with the mouse to rotate
, resolution 1.92Å
Sites: and
Ligands: , and
Activity: L-fuculose-phosphate aldolase, with EC number 4.1.2.17
Coordinates: save as pdb, mmCIF, xml



L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T


OverviewOverview

The structure of the class II zinc-ion dependent L-fuculose-1-phosphate aldolase from Escherichia coli in its tetragonal crystal form has been established at 1.92 A resolution. The homotetrameric enzyme has a molecular mass of 4 x 24 kDa and follows C(4) symmetry. The structure model is exactly symmetrical, which contradicts an observed birefringence anomaly of the crystals. The four catalytic centers are located in deep clefts at the interfaces of adjacent subunits. The zinc ion is coordinated by three histidines and one glutamate in an almost tetrahedral arrangement. In contrast to numerous other catalytically competent zinc ions, there is no water molecule in the ligand sphere. Replacement of zinc by a cobalt ion caused only small structural changes. A search through the Protein Data Bank indicated that the chain fold is novel. Sequence homology searches revealed a significant similarity to the bacterial L-ribulose-5-phosphate 4-epimerase.

About this StructureAbout this Structure

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

ReferenceReference

Refined high-resolution structure of the metal-ion dependent L-fuculose-1-phosphate aldolase (class II) from Escherichia coli., Dreyer MK, Schulz GE, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1082-91. PMID:15299567

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