1xps: Difference between revisions
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==Overview== | ==Overview== | ||
The structures of a new crystal form of ribonuclease A and its, low-humidity variant, each containing two crystallographically independent, molecules, have been determined and refined. A detailed comparison of, these structures with those of the other known crystal forms of the, enzyme, which have different packing arrangements and solvent composition, leads to a meaningful delineation of the rigid and flexible regions of the, protein molecule and the nature of its plasticity. Many of the water, molecules which are common to all the structures are involved in bridging, different regions of the protein molecule, thus emphasizing the role of, water in stabilizing the tertiary structure. The analysis of the, structures shows that for a given N or O atom, the level of hydration, increases ... | The structures of a new crystal form of ribonuclease A and its, low-humidity variant, each containing two crystallographically independent, molecules, have been determined and refined. A detailed comparison of, these structures with those of the other known crystal forms of the, enzyme, which have different packing arrangements and solvent composition, leads to a meaningful delineation of the rigid and flexible regions of the, protein molecule and the nature of its plasticity. Many of the water, molecules which are common to all the structures are involved in bridging, different regions of the protein molecule, thus emphasizing the role of, water in stabilizing the tertiary structure. The analysis of the, structures shows that for a given N or O atom, the level of hydration, increases with accessible surface area, but levels off at an area of about, 10 A2. Generally, the hydration level tends to drop when the area, increases beyond about 20 A2. This drop correlates with an increase in the, displacement parameter. The analysis also suggests that the van der Waals, radii and probe radius normally used in accessible surface area, calculations are not appropriate for dealing with all situations. | ||
==About this Structure== | ==About this Structure== | ||
1XPS is a | 1XPS 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] Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XPS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase (phosphoric diester)]] | [[Category: hydrolase (phosphoric diester)]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:02:43 2007'' | ||
Revision as of 14:57, 5 November 2007
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BOVINE RIBONUCLEASE A (PHOSPHATE-FREE) (93 % HUMIDITY)
OverviewOverview
The structures of a new crystal form of ribonuclease A and its, low-humidity variant, each containing two crystallographically independent, molecules, have been determined and refined. A detailed comparison of, these structures with those of the other known crystal forms of the, enzyme, which have different packing arrangements and solvent composition, leads to a meaningful delineation of the rigid and flexible regions of the, protein molecule and the nature of its plasticity. Many of the water, molecules which are common to all the structures are involved in bridging, different regions of the protein molecule, thus emphasizing the role of, water in stabilizing the tertiary structure. The analysis of the, structures shows that for a given N or O atom, the level of hydration, increases with accessible surface area, but levels off at an area of about, 10 A2. Generally, the hydration level tends to drop when the area, increases beyond about 20 A2. This drop correlates with an increase in the, displacement parameter. The analysis also suggests that the van der Waals, radii and probe radius normally used in accessible surface area, calculations are not appropriate for dealing with all situations.
About this StructureAbout this Structure
1XPS is a Single protein structure of sequence from Bos taurus. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Structure known Active Site: ACT. Full crystallographic information is available from OCA.
ReferenceReference
Plasticity, hydration and accessibility in ribonuclease A. The structure of a new crystal form and its low-humidity variant., Sadasivan C, Nagendra HG, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1343-52. PMID:10089510
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