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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1la2 ConSurf]. | ||
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Revision as of 04:32, 9 February 2016
Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthaseStructural analysis of Saccharomyces cerevisiae myo-inositol 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 PubMedThe New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex. Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase.,Kniewel R, Buglino JA, Shen V, Chadha T, Beckwith A, Lima CD J Struct Funct Genomics. 2002;2(3):129-34. PMID:12836703[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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