1jkf: Difference between revisions
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==Holo 1L-myo-inositol-1-phosphate Synthase== | ==Holo 1L-myo-inositol-1-phosphate Synthase== | ||
<StructureSection load='1jkf' size='340' side='right' caption='[[1jkf]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1jkf' size='340' side='right'caption='[[1jkf]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jkf]] 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=1JKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JKF FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jkf]] 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=1JKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JKF FirstGlance]. <br> | ||
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[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
[[Category: Inositol-3-phosphate synthase]] | [[Category: Inositol-3-phosphate synthase]] | ||
[[Category: Large Structures]] | |||
[[Category: Geiger, J H]] | [[Category: Geiger, J H]] | ||
[[Category: Stein, A J]] | [[Category: Stein, A J]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 12:25, 6 November 2019
Holo 1L-myo-inositol-1-phosphate SynthaseHolo 1L-myo-inositol-1-phosphate Synthase
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 PubMed1-l-myo-Inositol-1-phosphate synthase catalyzes the conversion of d-glucose 6-phosphate to 1-l-myo-inositol-1-phosphate (MIP), the first and rate-limiting step in the biosynthesis of all inositol-containing compounds. It involves an oxidation, intramolecular aldol cyclization, and reduction. We have determined the first crystal structure of MIP synthase. We present structures of both the NAD-bound enzyme and the enzyme bound to an inhibitor, 2-deoxy-glucitol-6-phosphate. While 58 amino acids are disordered in the unbound form of the enzyme in the vicinity of the active site, the inhibitor nucleates the folding of this domain in a striking example of induced fit, serving to completely encapsulate it within the enzyme. Three helices and a long beta-strand are formed in this process. We postulate a mechanism for the conversion based on the structure of the inhibitor-bound complex. The crystal structure and mechanism of 1-L-myo-inositol- 1-phosphate synthase.,Stein AJ, Geiger JH J Biol Chem. 2002 Mar 15;277(11):9484-91. Epub 2002 Jan 4. PMID:11779862[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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