1csm: Difference between revisions
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==THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION== | ==THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION== | ||
<StructureSection load='1csm' size='340' side='right' caption='[[1csm]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1csm' size='340' side='right'caption='[[1csm]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1csm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CSM FirstGlance]. <br> | <table><tr><td colspan='2'>[[1csm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CSM FirstGlance]. <br> | ||
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[[Category: Anthranilate synthase]] | [[Category: Anthranilate synthase]] | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | |||
[[Category: Lipscomb, W N]] | [[Category: Lipscomb, W N]] | ||
[[Category: Xue, Y]] | [[Category: Xue, Y]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
Revision as of 09:40, 10 October 2019
THE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTIONTHE CRYSTAL STRUCTURE OF ALLOSTERIC CHORISMATE MUTASE AT 2.2 ANGSTROMS RESOLUTION
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 PubMedThe crystal structure of an allosteric chorismate mutase, the Thr-226-->Ile mutant, from yeast Saccharomyces cerevisiae has been determined to 2.2-A resolution by using the multiple isomorphous replacement method. Solvent-flattening and electron-density modification were applied for phase improvement. The current crystallographic R factor is 0.196. The final model includes 504 of the 512 residues and 97 water molecules. In addition, two tryptophan molecules were identified in the interface between monomers. The overall structure is completely different from the reported structure of chorismate mutase from Bacillus subtilis. This structure showed 71% helices with essentially no beta-sheet structures. The crystal structure of allosteric chorismate mutase at 2.2-A resolution.,Xue Y, Lipscomb WN, Graf R, Schnappauf G, Braus G Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10814-8. PMID:7971967[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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