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    asheydina
    The two domains structure was found only in 3HRP protein which shown the 22% of sequence similarity with 3TC9 and 21% with 3KYA and also was solved by JCSG (GS 13221C). We were not able to find the same domain structure in either PDB, PFAM, SCOP, DALI and FATCAT data bases. To sum up, three proteins: 3TC9, 3KYA, 3HRP has similar structure where the N-terminal domain adopts an immunoglobulin-like fold and the C-terminal domain adopts a 6-bladed beta-propeller fold. The N-terminal immunoglobulin-like fold belongs to E set domains superfamily which are often found in cell surface receptors. In terms of structural similarity, the N-terminal domains show strong correlation with 1UAD (exocyst complex component Sec5), which belongs to GTP-binding proteins mediating the transmembrane signaling initiated by the occupancy of certain cell surface receptors, and two sugar-utilizing enzymes: Five-domain alpha-amylase from Bacillus Stearothermophilus (1QHO) and Maltose/acarbose complex cyclodextrin glycosyl transferase from Thermoanerobacterium thermosulfurigenes (3BMV). On the other hand, C-terminal domain shows strong structure similarity with a sensor domain of Serine/threonine-protein kinase PknD from Mycobacterium tuberculosis (1RWI). FFAS-SCOP score is -35.500, -29.500 and -40.300 for 3TC9, 3KYA, and 3HRP respectively. In spite of a significant structure similarity found with two enzymes: peptidyl-alpha-hydroxyglycine alpha-amidating lyase (3FVZ), where the active site is formed by a Zn(II) ion coordinated by three histidine residues (HIS585, HIS690,HIS786) and virginiamycin B lyase from Staphylococcus aureus (PDB code is 2Z2P) where the active site formed by a Mg(II) ion coordinated by HIS270, ASP127, GLU268, GLU284; sequence aliment and structure analysis didn’t show any conservative resides in the active sites positions. This fact let us to predict that C-terminal domain is a receptor or a sensor domain.

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