Sandbox1503
3vuf Protein(title here)
This is a default text for your page Sandbox1503. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue. ContentsFunction[SSG1_ORYSJ] Required for the synthesis of amylose in endosperm.[HAMAP-Rule:MF_00484] Publication Abstract from PubMedThe catalytic domain of rice (Oryza sativa japonica) granule bound starch synthase I (OsGBSSI-CD) was overexpressed and the three-dimensional structures of the ligand-free and ADP-bound forms were determined. The structures were similar to those reported for bacterial and archaeal glycogen synthases, which belong to glycosyltransferase family 5. They had Rossmann fold N- and C-domains connected by canonical two-hinge peptides, and an interdomain disulfide bond that appears to be conserved in the Poaceae plant family. The presence of three covalent linkages might explain why both OsGBSSI-CD structures adopted only the closed domain arrangement. Interdomain Disulfide Bridge in the Rice Granule Bound Starch Synthase I Catalytic Domain as Elucidated by X-Ray Structure Analysis.,Momma M, Fujimoto Z Biosci Biotechnol Biochem. 2012 Aug 7. PMID:22878205[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. DiseaseThe protein 3vuf has allergenic properties, for example in mammals it can binds to Immunoglobulin E (IgE) causing an allergic response. RelevanceStructural highlights
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References
Contents
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