3srn: Difference between revisions
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|PDB= 3srn |SIZE=350|CAPTION= <scene name='initialview01'>3srn</scene>, resolution 2.0Å | |PDB= 3srn |SIZE=350|CAPTION= <scene name='initialview01'>3srn</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3srn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3srn OCA], [http://www.ebi.ac.uk/pdbsum/3srn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3srn RCSB]</span> | |||
}} | }} | ||
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[[Category: Edwards, B F.P.]] | [[Category: Edwards, B F.P.]] | ||
[[Category: Martin, P D.]] | [[Category: Martin, P D.]] | ||
[[Category: hydrolase(nucleic acid,rna)]] | |||
[[Category: hydrolase(nucleic acid | |||
''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 05:36:07 2008'' | ||
Revision as of 05:36, 31 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Pancreatic ribonuclease, with EC number 3.1.27.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL CHANGES THAT ACCOMPANY THE REDUCED CATALYTIC EFFICIENCY OF TWO SEMISYNTHETIC RIBONUCLEASE ANALOGS
OverviewOverview
The structures of two catalytically defective semi-synthetic RNases obtained by replacing aspartic acid 121 with asparagine or alanine have been determined and refined at a resolution of 2.0 A (R = 0.186 and 0.172, respectively). When these structures are compared with the refined 1.8-A structure (R = 0.204) of the fully active aspartic acid-containing enzyme (Martin, P.D., Doscher, M.S., and Edwards, B. F. P. (1987) J. Biol. Chem. 262, 15930-15938), numerous and widespread changes, much greater in number and magnitude than the small structural variations noted previously between the semisynthetic complex and RNase A, are found to have occurred. These changes include the movement of the loop containing residues 65-72 away from the active site, a more or less generalized relocation of crystallographically bound water molecules, and a number of rearrangements in the hydrogen bonding network at the active site. Most changes are far removed from the immediate site of the modifications and are distributed essentially throughout the molecule. The details of many of these changes are unique to each analog. In the asparagine analog, a destabilization in the positioning of active site residue His-119 also appears to have occurred.
About this StructureAbout this Structure
3SRN is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs., deMel VS, Martin PD, Doscher MS, Edwards BF, J Biol Chem. 1992 Jan 5;267(1):247-56. PMID:1730593
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