1tri
From Proteopedia
(New page: 200px<br /><applet load="1tri" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tri, resolution 2.4Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:1tri.gif|left|200px]]<br /><applet load="1tri" size=" | + | [[Image:1tri.gif|left|200px]]<br /><applet load="1tri" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tri, resolution 2.4Å" /> | caption="1tri, resolution 2.4Å" /> | ||
'''THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP'''<br /> | '''THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The triosephosphate isomerase (TIM) fold is found in several | + | BACKGROUND: The triosephosphate isomerase (TIM) fold is found in several different classes of enzymes, most of which are oligomers; TIM itself always functions as a very tight dimer. It has recently been shown that a monomeric form of TIM ('monoTIM') can be constructed by replacing a 15-residue interface loop, loop-3, with an eight-residue fragment; modelling suggests that this should result in a short strain-free turn, resulting in the subsequent helix, helix-A3, having an additional turn at its amino terminus. RESULTS: The crystal structure of monoTIM shows that it retains the characteristic TIM-barrel (betaalpha)8-fold and that the new loop has a structure very close to that predicted. Two other interface loops, loop-1 and loop-4, which contain the active site residues Lys13 and His95, respectively, show significant changes in structure in monoTIM compared with dimeric wild-type TIM. CONCLUSION: The observed structural differences between monoTIM and wild-type TIM indicate that the dimeric appearance of TIM determines the location and conformation of two of the four catalytic residues. |
==About this Structure== | ==About this Structure== | ||
| - | 1TRI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1TRI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1TRI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
[[Category: Trypanosoma brucei brucei]] | [[Category: Trypanosoma brucei brucei]] | ||
| - | [[Category: Wierenga, R | + | [[Category: Wierenga, R K.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: isomerase(intramolecular oxidoreductase)]] | [[Category: isomerase(intramolecular oxidoreductase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:42 2008'' |
Revision as of 13:16, 21 February 2008
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THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP
Overview
BACKGROUND: The triosephosphate isomerase (TIM) fold is found in several different classes of enzymes, most of which are oligomers; TIM itself always functions as a very tight dimer. It has recently been shown that a monomeric form of TIM ('monoTIM') can be constructed by replacing a 15-residue interface loop, loop-3, with an eight-residue fragment; modelling suggests that this should result in a short strain-free turn, resulting in the subsequent helix, helix-A3, having an additional turn at its amino terminus. RESULTS: The crystal structure of monoTIM shows that it retains the characteristic TIM-barrel (betaalpha)8-fold and that the new loop has a structure very close to that predicted. Two other interface loops, loop-1 and loop-4, which contain the active site residues Lys13 and His95, respectively, show significant changes in structure in monoTIM compared with dimeric wild-type TIM. CONCLUSION: The observed structural differences between monoTIM and wild-type TIM indicate that the dimeric appearance of TIM determines the location and conformation of two of the four catalytic residues.
About this Structure
1TRI is a Single protein structure of sequence from Trypanosoma brucei brucei with as ligand. Active as Triose-phosphate isomerase, with EC number 5.3.1.1 Full crystallographic information is available from OCA.
Reference
The crystal structure of an engineered monomeric triosephosphate isomerase, monoTIM: the correct modelling of an eight-residue loop., Borchert TV, Abagyan R, Kishan KV, Zeelen JP, Wierenga RK, Structure. 1993 Nov 15;1(3):205-13. PMID:16100954
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