1tmh
From Proteopedia
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|PDB= 1tmh |SIZE=350|CAPTION= <scene name='initialview01'>1tmh</scene>, resolution 2.8Å | |PDB= 1tmh |SIZE=350|CAPTION= <scene name='initialview01'>1tmh</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
- | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tmh OCA], [http://www.ebi.ac.uk/pdbsum/1tmh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tmh RCSB]</span> | ||
}} | }} | ||
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[[Category: Wierenga, R K.]] | [[Category: Wierenga, R K.]] | ||
[[Category: Zeelen, J Ph.]] | [[Category: Zeelen, J Ph.]] | ||
- | [[Category: SO4]] | ||
[[Category: isomerase(intramolecular oxidoreductase)]] | [[Category: isomerase(intramolecular oxidoreductase)]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:58:10 2008'' |
Revision as of 20:58, 30 March 2008
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, resolution 2.8Å | |||||||
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Ligands: | |||||||
Activity: | Triose-phosphate isomerase, with EC number 5.3.1.1 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
MODULAR MUTAGENESIS OF A TIM-BARREL ENZYME: THE CRYSTAL STRUCTURE OF A CHIMERIC E. COLI TIM HAVING THE EIGHTH (BETA-ALPHA)-UNIT REPLACED BY THE EQUIVALENT UNIT OF CHICKEN TIM
Overview
The crystal structure of a hybrid Escherichia coli triosephosphate isomerase (TIM) has been determined at 2.8 A resolution. The hybrid TIM (ETIM8CHI) was constructed by replacing the eighth beta alpha-unit of E. coli TIM with the equivalent unit of chicken TIM. This replacement involves 10 sequence changes. One of the changes concerns the mutation of a buried alanine (Ala232 in strand 8) into a phenylalanine. The ETIM8CHI structure shows that the A232F sequence change can be incorporated by a side-chain rotation of Phe224 (in helix 7). No cavities or strained dihedrals are observed in ETIM8CHI in the region near position 232, which is in agreement with the observation that ETIM8CHI and E.coli TIM have similar stabilities. The largest CA (C-alpha atom) movements, approximately 3 A, are seen for the C-terminal end of helix 8 (associated with the outward rotation of Phe224) and for the residues in the loop after helix 1 (associated with sequence changes in helix 8). From the structure it is not clear why the kcat of ETIM8CHI is 10 times lower than in wild type E.coli TIM.
About this Structure
1TMH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Modular mutagenesis of a TIM-barrel enzyme: the crystal structure of a chimeric E. coli TIM having the eighth beta alpha-unit replaced by the equivalent unit of chicken TIM., Kishan R, Zeelen JP, Noble ME, Borchert TV, Mainfroid V, Goraj K, Martial JA, Wierenga RK, Protein Eng. 1994 Aug;7(8):945-51. PMID:7809033
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