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| - | [[Image:1u1b.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1u1b| PDB=1u1b | SCENE= }} | | {{STRUCTURE_1u1b| PDB=1u1b | SCENE= }} |
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| - | '''Structure of bovine pancreatic Ribonuclease A in complex with 3'-phosphothymidine (3'-5')-pyrophosphate adenosine 3'-phosphate'''
| + | ===Structure of bovine pancreatic Ribonuclease A in complex with 3'-phosphothymidine (3'-5')-pyrophosphate adenosine 3'-phosphate=== |
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| - | ==Overview==
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| - | Solution NMR spin-relaxation experiments were used to compare mus-ms dynamics in RNase A in the apo form and as complexed to the substrate-mimic, pTppAp. The crystal structure of the RNase A/pTppAp complex was determined and demonstrates that this ligand binds at the active site and utilizes established substrate binding sites in its interaction with RNase A. Relaxation-compensated CPMG experiments identify flexible residues in and around the active site in both the apo and pTppAp-bound enzyme. Quantitative analysis of the NMR spin-relaxation dispersion curves show that the time scale of motion in RNase A is unchanged when pTppAp binds and is similar to the time scale for the rate-determining step of the catalytic reaction. Temperature-dependent measurements provide an activation barrier for motion of 5.2 +/- 1.0 kcal/mol and 4.5 +/- 1.2 kcal/mol for the apo and pTppAp forms of RNase A, respectively. These data indicate very similar motion exists in the free and bound enzyme. Additionally, chemical shift data suggests that the magnitude of motion is also similar for these two forms and that it is likely that apo enzyme interconverts to a structure that resembles a ligand-bound form. Likewise, it appears that the bound conformation samples the apo enzyme form even when ligand is present. Taken together the data imply that RNase A is in a preexisting dynamic equilibrium between two conformations that represent the open and closed enzyme forms. These data suggest that ligand binding stabilizes the bound conformer but does not induce it.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15969595}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15969595 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15969595}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Nucleotide inhibitor]] | | [[Category: Nucleotide inhibitor]] |
| | [[Category: Ribonuclease]] | | [[Category: Ribonuclease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:37:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:18:22 2008'' |
Revision as of 07:18, 28 July 2008
Template:STRUCTURE 1u1b
Structure of bovine pancreatic Ribonuclease A in complex with 3'-phosphothymidine (3'-5')-pyrophosphate adenosine 3'-phosphate
Template:ABSTRACT PUBMED 15969595
About this Structure
1U1B is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Conservation of mus-ms enzyme motions in the apo- and substrate-mimicked state., Beach H, Cole R, Gill ML, Loria JP, J Am Chem Soc. 2005 Jun 29;127(25):9167-76. PMID:15969595
Page seeded by OCA on Mon Jul 28 10:18:22 2008
