1rhb: Difference between revisions

Revision as of 14:23, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rhb.png

Template:STRUCTURE 1rhb

WATER DEPENDENT DOMAIN MOTION AND FLEXIBILITY IN RIBONUCLEASE A AND THE INVARIANT FEATURES IN ITS HYDRATION SHELL. AN X-RAY STUDY OF TWO LOW HUMIDITY CRYSTAL FORMS OF THE ENZYMEWATER DEPENDENT DOMAIN MOTION AND FLEXIBILITY IN RIBONUCLEASE A AND THE INVARIANT FEATURES IN ITS HYDRATION SHELL. AN X-RAY STUDY OF TWO LOW HUMIDITY CRYSTAL FORMS OF THE ENZYME

Template:ABSTRACT PUBMED 15299799

About this StructureAbout this Structure

1RHB is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Water-dependent domain motion and flexibility in ribonuclease A and the invariant features in its hydration shell. An X-ray study of two low-humidity crystal forms of the enzyme., Kishan RV, Chandra NR, Sudarsanakumar C, Suguna K, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):703-10. PMID:15299799

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OCA

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-'''WATER DEPENDENT DOMAIN MOTION AND FLEXIBILITY IN RIBONUCLEASE A AND THE INVARIANT FEATURES IN ITS HYDRATION SHELL. AN X-RAY STUDY OF TWO LOW HUMIDITY CRYSTAL FORMS OF THE ENZYME'''
+===WATER DEPENDENT DOMAIN MOTION AND FLEXIBILITY IN RIBONUCLEASE A AND THE INVARIANT FEATURES IN ITS HYDRATION SHELL. AN X-RAY STUDY OF TWO LOW HUMIDITY CRYSTAL FORMS OF THE ENZYME===
-==Overview==
+<!--
-The crystal structures of 88 and 79% relative humidity forms of ribonuclease A, resulting from water-mediated transformations, have been refined employing the restrained least-squares method using X-ray data collected on an area detector to R = 0.173 for 15 326 observed reflections in the 10-1.5 A resolution shell and R = 0.176 for 8534 observed reflections in the 10-1.8 A shell, respectively. The comparison of these structures with those of the native, the phosphate-bound and the sulfate-bound forms demonstrates that the mobility of the ribonuclease A molecule involves hinge-bending movement of the two domains and local flexibility within them, particularly at the termini of regular secondary structures and in loops. The comparison also leads to the identification of 31 invariant water molecules in the hydration shell of the enzyme, many of which are involved in holding different parts of the molecule together and in stabilizing local structure. The conformational changes that accompany the partial removal of the surrounding water, particularly those observed in the 79% form, could be similar to those that occur during enzyme action.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299799}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299799 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15299799}}
 ==About this Structure==
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 [[Category: Suguna, K.]]
 [[Category: Vijayan, M.]]
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