1fba

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{{STRUCTURE_1fba| PDB=1fba | SCENE= }}
{{STRUCTURE_1fba| PDB=1fba | SCENE= }}
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'''THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM DROSOPHILA MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION'''
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===THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM DROSOPHILA MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION===
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==Overview==
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The structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster has been determined by X-ray diffraction at 2.5 A resolution. The insect enzyme crystallizes in space group P2(1)2(1)2(1) with lattice replacement with rabbit muscle aldolase as a search model has been employed to solve the structure. To improve the initial phases real space averaging, including phase extension from 4.0 to 2.5 A, has been applied. Refinement of the atomic positions by molecular dynamics resulted in a crystallographic R-factor of 0.214. The tertiary structure resembles in most parts that of the vertebrate aldolase from rabbit muscle. Significant differences were found in surface loops and the N- and C-terminal regions of the protein. Here we present the first aldolase structure where the functionally important C-terminal arm is described completely.
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{{ABSTRACT_PUBMED_1959612}}
==About this Structure==
==About this Structure==
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[[Category: Hester, G.]]
[[Category: Hester, G.]]
[[Category: Piontek, K.]]
[[Category: Piontek, K.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:59:25 2008''

Revision as of 23:59, 30 June 2008

Template:STRUCTURE 1fba

THE CRYSTAL STRUCTURE OF FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM DROSOPHILA MELANOGASTER AT 2.5 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 1959612

About this Structure

1FBA is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

Reference

The crystal structure of fructose-1,6-bisphosphate aldolase from Drosophila melanogaster at 2.5 A resolution., Hester G, Brenner-Holzach O, Rossi FA, Struck-Donatz M, Winterhalter KH, Smit JD, Piontek K, FEBS Lett. 1991 Nov 4;292(1-2):237-42. PMID:1959612

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