1tre
From Proteopedia
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| - | [[Image:1tre.gif|left|200px]] | + | [[Image:1tre.gif|left|200px]] |
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| - | '''THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION''' | + | {{Structure |
| + | |PDB= 1tre |SIZE=350|CAPTION= <scene name='initialview01'>1tre</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM ESCHERICHIA COLI DETERMINED AT 2.6 ANGSTROM RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TRE is a [ | + | 1TRE 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=1TRE OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15299515 15299515] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: intramolecular oxidoreductase]] | [[Category: intramolecular oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:22:09 2008'' |
Revision as of 12:22, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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