1hz1: Difference between revisions
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==RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+== | ==RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+== | ||
<StructureSection load='1hz1' size='340' side='right' caption='[[1hz1]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1hz1' size='340' side='right'caption='[[1hz1]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hz1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HZ1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1hz1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HZ1 FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | |||
*[[Temp|Temp]] | *[[Temp|Temp]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: A. niger]] | [[Category: A. niger]] | ||
[[Category: Large Structures]] | |||
[[Category: Langhorst, U]] | [[Category: Langhorst, U]] | ||
[[Category: Loris, R]] | [[Category: Loris, R]] | ||
Revision as of 13:14, 30 October 2019
RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+RIBONUCLEASE T1 V16A MUTANT IN COMPLEX WITH MG2+
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn the crystalline state, ribonuclease T1 binds calcium ions at different lattice-dependent positions. In solution, its conformational stability is also remarkably increased in the presence of divalent metal ions. Combining urea unfolding studies and X-ray crystallography, we compared the presence of several metal ions at specific sites in the protein to their contribution to the overall stabilizing effect in solution. We constructed thermodynamic cycles involving particular metal ions and specific carboxylate functions. The resulting coupling energies indicate that some (but not all) metal ions found at lattice contacts in crystal structures may indeed significantly contribute to stability enhancement in the presence of metal ions in solution. The contribution of metal ions to the conformational stability of ribonuclease T1: crystal versus solution.,Deswarte J, De Vos S, Langhorst U, Steyaert J, Loris R Eur J Biochem. 2001 Jul;268(14):3993-4000. PMID:11453993[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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