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1iyy
From Proteopedia
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| - | [[Image:1iyy.jpg|left|200px]] | + | [[Image:1iyy.jpg|left|200px]] |
| - | + | ||
| - | '''NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1iyy |SIZE=350|CAPTION= <scene name='initialview01'>1iyy</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IYY is a [ | + | 1IYY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_oryzae Aspergillus oryzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IYY OCA]. |
==Reference== | ==Reference== | ||
| - | Determination of the NMR structure of Gln25-ribonuclease T1., Hatano K, Kojima M, Suzuki E, Tanokura M, Takahashi K, Biol Chem. 2003 Aug;384(8):1173-83. PMID:[http:// | + | Determination of the NMR structure of Gln25-ribonuclease T1., Hatano K, Kojima M, Suzuki E, Tanokura M, Takahashi K, Biol Chem. 2003 Aug;384(8):1173-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12974386 12974386] |
[[Category: Aspergillus oryzae]] | [[Category: Aspergillus oryzae]] | ||
[[Category: Ribonuclease T(1)]] | [[Category: Ribonuclease T(1)]] | ||
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[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:56:46 2008'' |
Revision as of 09:56, 20 March 2008
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| Activity: | Ribonuclease T(1), with EC number 3.1.27.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF Gln25-RIBONUCLEASE T1, 24 STRUCTURES
Overview
Ribonuclease (RNase) T1 is a guanyloribonuclease, having two isozymes in nature, Gln25- and Lys25-RNase T1. Between these two isozymes, there is no difference in catalytic activity and three-dimensional structure; however, Lys25-RNase T1 is slightly more stable than Gln25-RNase T1. Recently, it has been suggested that the existence of a salt bridge between Lys25 and Asp29/Glu31 in Lys25-RNase T1 contributes to the stability. To elucidate the effects of the replacement of Lys25 with a Gln on the conformation and microenvironments of RNase T1 in detail, the three-dimensional solution structure of Gln25-RNase T1 was determined by simulated-annealing calculations. As a result, the topology of the overall folding was shown to be very similar to that of the Lys25-isozyme except for some differences. In particular, there were two differences in the property of torsion angles of the two disulfide bonds and the conformations of the residues 11-13, 63-66, and 92-93. With regard to the residues 11-13, the lack of the above-mentioned salt bridge in Gln25-RNase T1 was thought to induce the conformational difference of this segment as compared with the Lys25-isozyme. Furthermore, it was proposed that the perturbation of this segment might transfer to the residues 92-93 via the two disulfide bonds.
About this Structure
1IYY is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
Reference
Determination of the NMR structure of Gln25-ribonuclease T1., Hatano K, Kojima M, Suzuki E, Tanokura M, Takahashi K, Biol Chem. 2003 Aug;384(8):1173-83. PMID:12974386
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