1sw0: Difference between revisions

New page: left|200px<br /><applet load="1sw0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sw0, resolution 1.71Å" /> '''Triosephosphate isom...
 
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'''Triosephosphate isomerase from Gallus gallus, loop 6 hinge mutant K174L, T175W'''<br />
'''Triosephosphate isomerase from Gallus gallus, loop 6 hinge mutant K174L, T175W'''<br />


==Overview==
==Overview==
The conformational switch from open to closed of the flexible loop 6 of, triosephosphate isomerase (TIM) is essential for the catalytic properties, of TIM. Using a directed evolution approach, active variants of chicken, TIM with a mutated C-terminal hinge tripeptide of loop 6 have been, generated (Sun,J. and Sampson,N.S., Biochemistry, 1999, 38, 11474-11481)., In chicken TIM, the wild-type C-terminal hinge tripeptide is KTA. Detailed, enzymological characterization of six variants showed that some of these, (LWA, NPN, YSL, KTK) have decreased catalytic efficiency, whereas others, (KVA, NSS) are essentially identical with wild-type. The structural, characterization of these six variants is reported. No significant, structural differences compared with the wild-type are found for KVA, NSS, and LWA, but substantial structural adaptations are seen for NPN, YSL and, KTK. These structural differences can be understood from the buried, position of the alanine side chain in the C-hinge position 3 in the open, conformation of wild-type loop 6. Replacement of this alanine with a bulky, side chain causes the closed conformation to be favored, which correlates, with the decreased catalytic efficiency of these variants. The structural, context of loop 6 and loop 7 and their sequence conservation in 133, wild-type sequences is also discussed.
The conformational switch from open to closed of the flexible loop 6 of triosephosphate isomerase (TIM) is essential for the catalytic properties of TIM. Using a directed evolution approach, active variants of chicken TIM with a mutated C-terminal hinge tripeptide of loop 6 have been generated (Sun,J. and Sampson,N.S., Biochemistry, 1999, 38, 11474-11481). In chicken TIM, the wild-type C-terminal hinge tripeptide is KTA. Detailed enzymological characterization of six variants showed that some of these (LWA, NPN, YSL, KTK) have decreased catalytic efficiency, whereas others (KVA, NSS) are essentially identical with wild-type. The structural characterization of these six variants is reported. No significant structural differences compared with the wild-type are found for KVA, NSS and LWA, but substantial structural adaptations are seen for NPN, YSL and KTK. These structural differences can be understood from the buried position of the alanine side chain in the C-hinge position 3 in the open conformation of wild-type loop 6. Replacement of this alanine with a bulky side chain causes the closed conformation to be favored, which correlates with the decreased catalytic efficiency of these variants. The structural context of loop 6 and loop 7 and their sequence conservation in 133 wild-type sequences is also discussed.


==About this Structure==
==About this Structure==
1SW0 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 PGA 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=1SW0 OCA].  
1SW0 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=PGA:'>PGA</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=1SW0 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Triose-phosphate isomerase]]
[[Category: Triose-phosphate isomerase]]
[[Category: Haapalainen, A.M.]]
[[Category: Haapalainen, A M.]]
[[Category: Kursula, I.]]
[[Category: Kursula, I.]]
[[Category: Norledge, B.V.]]
[[Category: Norledge, B V.]]
[[Category: Salin, M.]]
[[Category: Salin, M.]]
[[Category: Sampson, N.S.]]
[[Category: Sampson, N S.]]
[[Category: Sun, J.]]
[[Category: Sun, J.]]
[[Category: Wierenga, R.K.]]
[[Category: Wierenga, R K.]]
[[Category: PGA]]
[[Category: PGA]]
[[Category: flexible loop]]
[[Category: flexible loop]]
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[[Category: tim barrel]]
[[Category: tim barrel]]


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