1i2f
From Proteopedia
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|PDB= 1i2f |SIZE=350|CAPTION= <scene name='initialview01'>1i2f</scene>, resolution 1.95Å | |PDB= 1i2f |SIZE=350|CAPTION= <scene name='initialview01'>1i2f</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=2GP:GUANOSINE-2'-MONOPHOSPHATE'>2GP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1i2e|1I2E]], [[1i2g|1I2G]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i2f OCA], [http://www.ebi.ac.uk/pdbsum/1i2f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i2f RCSB]</span> | ||
}} | }} | ||
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[[Category: Steyaert, J.]] | [[Category: Steyaert, J.]] | ||
[[Category: Vos, S De.]] | [[Category: Vos, S De.]] | ||
| - | [[Category: 2GP]] | ||
| - | [[Category: CA]] | ||
[[Category: cavity creation]] | [[Category: cavity creation]] | ||
[[Category: hydrophobic core packing]] | [[Category: hydrophobic core packing]] | ||
[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:13:38 2008'' |
Revision as of 18:13, 30 March 2008
| |||||||
| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||
| Related: | 1I2E, 1I2G
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ribonuclease T1 V16A mutant, form II
Overview
Differential scanning calorimetry, urea denaturation, and X-ray crystallography were combined to study the structural and energetic consequences of refilling an engineered cavity in the hydrophobic core of RNase T1 with CH(3), SH, and OH groups. Three valines that cluster together in the major hydrophobic core of T1 were each replaced with Ala, Ser, Thr, and Cys. Compared to the wild-type protein, all these mutants reduce the thermodynamic stability of the enzyme considerably. The relative order of stability at all three positions is as follows: Val > Ala approximately equal to Thr > Ser. The effect of introducing a sulfhydryl group is more variable. Surprisingly, a Val --> Cys mutation in a hydrophobic environment can be as or even more destabilizing than a Val --> Ser mutation. Furthermore, our results reveal that the penalty for introducing an OH group into a hydrophobic cavity is roughly the same as the gain obtained from filling the cavity with a CH(3) group. The inverse equivalence of the behavior of hydroxyl and methyl groups seems to be crucial for the unique three-dimensional structure of the proteins. The importance of negative design elements in this context is highlighted.
About this Structure
1I2F is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
Reference
Hydrophobic core manipulations in ribonuclease T1., De Vos S, Backmann J, Prevost M, Steyaert J, Loris R, Biochemistry. 2001 Aug 28;40(34):10140-9. PMID:11513591
Page seeded by OCA on Sun Mar 30 21:13:38 2008
