Source:http://linkedlifedata.com/resource/pubmed/id/11856829
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 3
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pubmed:dateCreated |
2002-3-7
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/PDB/1KF2,
http://linkedlifedata.com/resource/pubmed/xref/PDB/1KF3,
http://linkedlifedata.com/resource/pubmed/xref/PDB/IKF4,
http://linkedlifedata.com/resource/pubmed/xref/PDB/IKF5,
http://linkedlifedata.com/resource/pubmed/xref/PDB/IKF7,
http://linkedlifedata.com/resource/pubmed/xref/PDB/IKF8
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pubmed:abstractText |
The diffraction pattern of protein crystals extending to atomic resolution guarantees a very accurate picture of the molecular structure and enables the study of subtle phenomena related to protein functionality. Six structures of bovine pancreatic ribonuclease at the pH* values 5.2, 5.9, 6.3, 7.1, 8.0 and 8.8 and at resolution limits in the range 1.05-1.15A have been refined. An overall description of the six structures and several aspects, mainly regarding pH-triggered conformational changes, are described here. Since subtle variations were expected, a thorough validation assessment of the six refined models was first carried out. Some stereochemical parameters, such as the N[bond]C(alpha)[bond]C angle and the pyramidalization at the carbonyl C atoms, indicate that the standard target values and their weights typically used in refinement may need revision. A detailed comparison of the six structures has provided experimental evidence on the role of Lys41 in catalysis. Furthermore, insights are given into the structural effects related to the pH-dependent binding of a sulfate anion, which mimics the phosphate group of RNA, in the active site. Finally, the results support a number of thermodynamic and kinetic experimental data concerning the role of the disulfide bridge between Cys65 and Cys72 in the folding of RNase A.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease, Pancreatic,
http://linkedlifedata.com/resource/pubmed/chemical/Solvents
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
441-50
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:11856829-Animals,
pubmed-meshheading:11856829-Catalytic Domain,
pubmed-meshheading:11856829-Cattle,
pubmed-meshheading:11856829-Crystallization,
pubmed-meshheading:11856829-Crystallography, X-Ray,
pubmed-meshheading:11856829-Disulfides,
pubmed-meshheading:11856829-Hydrogen-Ion Concentration,
pubmed-meshheading:11856829-Ligands,
pubmed-meshheading:11856829-Lysine,
pubmed-meshheading:11856829-Models, Molecular,
pubmed-meshheading:11856829-Protein Conformation,
pubmed-meshheading:11856829-Protein Folding,
pubmed-meshheading:11856829-Ribonuclease, Pancreatic,
pubmed-meshheading:11856829-Solvents
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pubmed:year |
2002
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pubmed:articleTitle |
Atomic resolution structures of ribonuclease A at six pH values.
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pubmed:affiliation |
Centro di Studio di Biocristallografia, CNR, Via Mezzocannone 6, I-80134 Napoli, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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