1fua

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==Overview==
==Overview==
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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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15299567 (full description)]]
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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 Structure==
==About this Structure==
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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 ZN, SO4 and BME 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]]. Structure known Active Sites: ACT and PBS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FUA OCA]].
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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 ZN, SO4 and BME 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] Structure known Active Sites: ACT and PBS. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FUA OCA].
==Reference==
==Reference==
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[[Category: zinc enzyme]]
[[Category: zinc enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:12:49 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:55:35 2007''

Revision as of 12:50, 5 November 2007


1fua, resolution 1.92Å

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L-FUCULOSE 1-PHOSPHATE ALDOLASE CRYSTAL FORM T

Overview

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 Structure

1FUA is a Single protein structure of sequence from Escherichia coli with ZN, SO4 and BME as ligands. Active as L-fuculose-phosphate aldolase, with EC number 4.1.2.17 Structure known Active Sites: ACT and PBS. Full crystallographic information is available from OCA.

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:15299567

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