1tri: Difference between revisions

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[[Image:1tri.gif|left|200px]]<br /><applet load="1tri" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1tri.gif|left|200px]]
caption="1tri, resolution 2.4&Aring;" />
 
'''THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP'''<br />
{{Structure
|PDB= 1tri |SIZE=350|CAPTION= <scene name='initialview01'>1tri</scene>, resolution 2.4&Aring;
|SITE=
|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]
|GENE=
}}
 
'''THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP'''
 


==Overview==
==Overview==
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==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 <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].  
1TRI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei Trypanosoma brucei brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TRI OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16100954 16100954]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16100954 16100954]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Triose-phosphate isomerase]]
[[Category: Triose-phosphate isomerase]]
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[[Category: isomerase(intramolecular oxidoreductase)]]
[[Category: isomerase(intramolecular oxidoreductase)]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:16:42 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:22:16 2008''

Revision as of 15:22, 20 March 2008

File:1tri.gif


PDB ID 1tri

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands:
Activity: Triose-phosphate isomerase, with EC number 5.3.1.1
Coordinates: save as pdb, mmCIF, xml



THE CRYSTAL STRUCTURE OF AN ENGINEERED MONOMERIC TRIOSEPHOSPHATE ISOMERASE, MONOTIM: THE CORRECT MODELLING OF AN EIGHT-RESIDUE LOOP


OverviewOverview

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 StructureAbout this Structure

1TRI is a Single protein structure of sequence from Trypanosoma brucei brucei. Full crystallographic information is available from OCA.

ReferenceReference

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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