Sandbox1503
3vuf Protein(title here)3vuf Protein(title here)
3vuf is a 1 chain structure protein which is synthesized by the Japanese rice (Oryza sativa japonica). it’s an enzyme, more accurately a transferase. It’s a NDP-glucose--starch glucosyltransferase, which is involved in the synthesis of amylose in the rice. This enzyme is located chloroplast and in amyloplast. The 3vuf protein is 609 amino acids long and weighs 66 476 Da. FunctionThe protein have a role of transferase, more accurately it is a NDP-glucose--starch glucosyltransferase, which catalyse the reaction below : This is a reaction allowing the extension of amylose. It has a major role in the pathway starch biosynthesis.
[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[1] 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 bind to Immunoglobulin E (IgE) causing an allergic response. RelevanceStructurePrimary structure (amino acid sequence):
MSALTTSQLA TSATGFGIAD RSAPSSLLRH GFQGLKPRSP AGGDATSLSV TTSARATPKQ QRSVQRGSRR FPSVVVYATG AGMNVVFVGA EMAPWSKTGG LGDVLGGLPP AMAANGHRVM VISPRYDQYK DAWDTSVVAE IKVADRYERV RFFHCYKRGV DRVFIDHPSF LEKVWGKTGE KIYGPDTGVD YKDNQMRFSL LCQAALEAPR ILNLNNNPYF KGTYGEDVVF VCNDWHTGPL ASYLKNNYQP NGIYRNAKVA FCIHNISYQG RFAFEDYPEL NLSERFRSSF DFIDGYDTPV EGRKINWMKA GILEADRVLT VSPYYAEELI SGIARGCELD NIMRLTGITG IVNGMDVSEW DPSKDKYITA KYDATTAIEA KALNKEALQA EAGLPVDRKI PLIAFIGRLE EQKGPDVMAA AIPELMQEDV QIVLLGTGKK KFEKLLKSME EKYPGKVRAV VKFNAPLAHL IMAGADVLAV PSRFEPCGLI QLQGMRYGTP CACASTGGLV DTVIEGKTGF HMGRLSVDCK VVEPSDVKKV AATLKRAIKV VGTPAYEEMV RNCMNQDLSW KGPAKNWENV LLGLGVAGSA PGIEGDEIAP LAKENVAAP
Secondary structure: Structural highlightsThis protein is an enzyme, which is formed from one monomer and can bind to ADP. It binds to the ADP-glucose with amino acids 97,100, 408, 413,462 and 492. This allow the formation of an hydrophobic pocket in which ADP-glucose can binds to and in which he is protected from water and hydrolyse. we can also see that 3vuf can binds sulfate. This hydrophobic cage is allowed by the beta sheets and alpha helices that the protein have.
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ReferencesReferences
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