2ea1
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GPG:GUANYLYL-2',5'-PHOSPHOGUANOSINE'>GPG</scene> | |LIGAND= <scene name='pdbligand=GPG:GUANYLYL-2',5'-PHOSPHOGUANOSINE'>GPG</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Enterobacter_ribonuclease Enterobacter ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.6 3.1.27.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Enterobacter_ribonuclease Enterobacter ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.6 3.1.27.6] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ea1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ea1 OCA], [http://www.ebi.ac.uk/pdbsum/2ea1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ea1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pan, J.]] | [[Category: Pan, J.]] | ||
[[Category: Zhou, K.]] | [[Category: Zhou, K.]] | ||
| - | [[Category: GPG]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: protein-gpg complex]] | [[Category: protein-gpg complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:45:58 2008'' |
Revision as of 23:46, 30 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Enterobacter ribonuclease, with EC number 3.1.27.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Ribonuclease I from Escherichia coli COMPLEXED WITH GUANYLYL-2(PRIME),5(PRIME)-GUANOSINE
Overview
We have constructed a strain that overproduces ribonuclease I of Escherichia coli and we have purified large quantities of the enzyme. Data from fluorescence, CD, and DSC measurements showed that it was a very stable protein. The conformation energy determined from urea and guanidine hydrochloride denaturation experiments was 11.5 kcal mol(-1) at pH 7.5. Thermal denaturation studies indicated that it had a T(m) of 64 degrees C at pH 4.0. RNase I belongs to the RNase T2/S-RNase group of endoribonucleases, but near the amino terminus it has an unusually long hydrophilic segment. Part of this was removed in the deletion construct, RNase I Delta(26-38). We have obtained crystals of both RNase I and of an enzyme-G2'p5'G complex in the P2(1) space group and oligonucleotide complexes with both wild type and mutant enzymes. The current study lays the groundwork for extensive investigation into the structure, function, and physical properties of this widely distributed group of ribonucleases.
About this Structure
2EA1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Overexpression, biophysical characterization, and crystallization of ribonuclease I from Escherichia coli, a broad-specificity enzyme in the RNase T2 family., Padmanabhan S, Zhou K, Chu CY, Lim RW, Lim LW, Arch Biochem Biophys. 2001 Jun 1;390(1):42-50. PMID:11368513
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