2e7y: Difference between revisions
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==High resolution structure of T. maritima tRNase Z== | ==High resolution structure of T. maritima tRNase Z== | ||
<StructureSection load='2e7y' size='340' side='right' caption='[[2e7y]], [[Resolution|resolution]] 1.97Å' scene=''> | <StructureSection load='2e7y' size='340' side='right'caption='[[2e7y]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2e7y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E7Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[2e7y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2E7Y FirstGlance]. <br> | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
*[[Temp|Temp]] | *[[Temp|Temp]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43589]] | [[Category: Atcc 43589]] | ||
[[Category: Large Structures]] | |||
[[Category: Ribonuclease Z]] | [[Category: Ribonuclease Z]] | ||
[[Category: Ishii, R]] | [[Category: Ishii, R]] | ||
Revision as of 11:28, 11 March 2020
High resolution structure of T. maritima tRNase ZHigh resolution structure of T. maritima tRNase Z
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 PubMedtRNA 3'-processing endoribonuclease (tRNase Z) is one of the enzymes involved in the 3'-end processing of precursor tRNAs and is a member of the metallo-beta-lactamase superfamily. tRNase Z crystal structures have revealed that the enzyme forms a dimer and has a characteristic domain, named a flexible arm or an exosite, which protrudes from the metallo-beta-lactamase core and is involved in tRNA binding. The refined structure of Thermotoga maritima tRNase Z has been determined at 1.97 A resolution, revealing the structure of the flexible arm and the zinc-bound active site. The structure of the flexible arm of T. maritima tRNase Z is distinct from those of the Bacillus subtilis and Escherichia coli tRNase Zs. A comparison of the three tRNase Z structures revealed differences in the dimer orientation, which may be related to the unique cleavage-site specificity of T. maritima tRNase Z. The structure of the flexible arm of Thermotoga maritima tRNase Z differs from those of homologous enzymes.,Ishii R, Minagawa A, Takaku H, Takagi M, Nashimoto M, Yokoyama S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):637-41. Epub 2007 Jul 21. PMID:17671357[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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