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New page: left|200px<br /><applet load="1tph" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tph, resolution 1.8Å" /> '''1.8 ANGSTROMS CRYSTAL...
 
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[[Image:1tph.gif|left|200px]]<br /><applet load="1tph" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1tph.gif|left|200px]]<br /><applet load="1tph" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1tph, resolution 1.8&Aring;" />
caption="1tph, resolution 1.8&Aring;" />
'''1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX'''<br />
'''1.8 ANGSTROMS CRYSTAL STRUCTURE OF WILD TYPE CHICKEN TRIOSEPHOSPHATE ISOMERASE-PHOSPHOGLYCOLOHYDROXAMATE COMPLEX'''<br />


==Overview==
==Overview==
The crystal structure of recombinant chicken triosephosphate isomerase, (TIM, E.C. 5.3.1.1) complexed with the intermediate analogue, phosphoglycolohydroxamate (PGH) has been solved by the method of molecular, replacement and refined to an R-factor of 18.5% at 1.8-A resolution. The, structure is essentially identical to that of the yeast TIM-PGH complex, [Davenport, R. C., et al. (1991) Biochemistry 30, 5821-5826] determined, earlier and refined at comparable resolution. This identity extends to the, high-energy conformations of the active-site residues Lys13 and Ser211, as, well as the positions of several bound water molecules that are retained, in the active site when PGH is bound. Comparison with the structure of, uncomplexed chicken TIM shows that the catalytic base, Glu165, moves, several angstroms when PGH binds. This movement may provide a trigger for, a larger conformational change, one of 7 A, in a loop near the active, site, which folds down like a lid to shield the bound inhibitor and, catalytic residues from contact with bulk solvent. These same, conformational changes were seen in crystalline yeast TIM upon binding of, PGH; their occurrence here in a different crystal form of TIM eliminates, the possibility that they are an artifact of crystal packing.
The crystal structure of recombinant chicken triosephosphate isomerase (TIM, E.C. 5.3.1.1) complexed with the intermediate analogue phosphoglycolohydroxamate (PGH) has been solved by the method of molecular replacement and refined to an R-factor of 18.5% at 1.8-A resolution. The structure is essentially identical to that of the yeast TIM-PGH complex [Davenport, R. C., et al. (1991) Biochemistry 30, 5821-5826] determined earlier and refined at comparable resolution. This identity extends to the high-energy conformations of the active-site residues Lys13 and Ser211, as well as the positions of several bound water molecules that are retained in the active site when PGH is bound. Comparison with the structure of uncomplexed chicken TIM shows that the catalytic base, Glu165, moves several angstroms when PGH binds. This movement may provide a trigger for a larger conformational change, one of 7 A, in a loop near the active site, which folds down like a lid to shield the bound inhibitor and catalytic residues from contact with bulk solvent. These same conformational changes were seen in crystalline yeast TIM upon binding of PGH; their occurrence here in a different crystal form of TIM eliminates the possibility that they are an artifact of crystal packing.


==About this Structure==
==About this Structure==
1TPH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with PGH 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TPH OCA].  
1TPH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=PGH:'>PGH</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=1TPH OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Triose-phosphate isomerase]]
[[Category: Triose-phosphate isomerase]]
[[Category: Knowles, J.R.]]
[[Category: Knowles, J R.]]
[[Category: Komives, E.A.]]
[[Category: Komives, E A.]]
[[Category: Liu, K.D.]]
[[Category: Liu, K D.]]
[[Category: Petsko, G.A.]]
[[Category: Petsko, G A.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
[[Category: Sugio, S.]]
[[Category: Sugio, S.]]
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[[Category: triosephosphate isomerase]]
[[Category: triosephosphate isomerase]]


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