1tre
From Proteopedia
(New page: 200px<br /><applet load="1tre" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tre, resolution 2.6Å" /> '''THE STRUCTURE OF TRIO...) |
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| - | [[Image:1tre.gif|left|200px]]<br /><applet load="1tre" size=" | + | [[Image:1tre.gif|left|200px]]<br /><applet load="1tre" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tre, resolution 2.6Å" /> | caption="1tre, resolution 2.6Å" /> | ||
'''THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION'''<br /> | '''THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of triosephosphate isomerase (TIM) from the organism | + | The structure of triosephosphate isomerase (TIM) from the organism Escherichia coli has been determined at a resolution of 2.6 A. The structure was solved by the molecular replacement method, first at 2.8 A resolution with a crystal grown by the technique of hanging-drop crystallization from a mother liquor containing the transition-state analogue 2-phosphoglycolate (2PG). As a search model in the molecular replacement calculations, the refined structure of TIM from Trypanosoma brucei, which has a sequence identity of 46% compared to the enzyme from E. coli, was used. An E. coli TIM crystal grown in the absence of 2PG, diffracting to 2.6 A resolution, was later obtained by application of the technique of macro-seeding using a seed crystal grown from a mother liquor without 2PG. The final 2.6 A model has a crystallographic R factor of 11.9%, and agrees well with standard stereochemical parameters. The structure of E. coli TIM suggests the importance of residues which favour helix initiation for the formation of the TIM fold. In addition, TIM from E. coli shows peculiarities in its dimer interface, and in the packing of core residues within the beta-barrel. |
==About this Structure== | ==About this Structure== | ||
| - | 1TRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http:// | + | 1TRE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
| - | [[Category: Noble, M | + | [[Category: Noble, M E.M.]] |
| - | [[Category: Wierenga, R | + | [[Category: Wierenga, R K.]] |
[[Category: intramolecular oxidoreductase]] | [[Category: intramolecular oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:37 2008'' |
Revision as of 13:16, 21 February 2008
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THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION
Overview
The structure of triosephosphate isomerase (TIM) from the organism Escherichia coli has been determined at a resolution of 2.6 A. The structure was solved by the molecular replacement method, first at 2.8 A resolution with a crystal grown by the technique of hanging-drop crystallization from a mother liquor containing the transition-state analogue 2-phosphoglycolate (2PG). As a search model in the molecular replacement calculations, the refined structure of TIM from Trypanosoma brucei, which has a sequence identity of 46% compared to the enzyme from E. coli, was used. An E. coli TIM crystal grown in the absence of 2PG, diffracting to 2.6 A resolution, was later obtained by application of the technique of macro-seeding using a seed crystal grown from a mother liquor without 2PG. The final 2.6 A model has a crystallographic R factor of 11.9%, and agrees well with standard stereochemical parameters. The structure of E. coli TIM suggests the importance of residues which favour helix initiation for the formation of the TIM fold. In addition, TIM from E. coli shows peculiarities in its dimer interface, and in the packing of core residues within the beta-barrel.
About this Structure
1TRE is a Single protein structure of sequence from Escherichia coli. Active as Triose-phosphate isomerase, with EC number 5.3.1.1 Full crystallographic information is available from OCA.
Reference
Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution., Noble ME, Zeelen JP, Wierenga RK, Mainfroid V, Goraj K, Gohimont AC, Martial JA, Acta Crystallogr D Biol Crystallogr. 1993 Jul 1;49(Pt 4):403-17. PMID:15299515
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