1rha

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[[Image:1rha.gif|left|200px]]<br /><applet load="1rha" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rha.gif|left|200px]]
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caption="1rha, resolution 1.8&Aring;" />
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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'''<br />
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{{Structure
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|PDB= 1rha |SIZE=350|CAPTION= <scene name='initialview01'>1rha</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND=
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|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]
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|GENE=
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}}
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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'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1RHA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RHA OCA].
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1RHA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RHA OCA].
==Reference==
==Reference==
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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., Kishan RV, Chandra NR, Sudarsanakumar C, Suguna K, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):703-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299799 15299799]
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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., Kishan RV, Chandra NR, Sudarsanakumar C, Suguna K, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):703-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299799 15299799]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Pancreatic ribonuclease]]
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[[Category: rna)]]
[[Category: rna)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:51:39 2008''

Revision as of 11:51, 20 March 2008


PDB ID 1rha

Drag the structure with the mouse to rotate
, resolution 1.8Å
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Coordinates: save as pdb, mmCIF, xml



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.

About this Structure

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

Reference

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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