5iaz: Difference between revisions
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The | ==The C-terminal domain of rice beta-galactosidase 1== | ||
<StructureSection load='5iaz' size='340' side='right' caption='[[5iaz]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5iaz]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IAZ FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5iaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iaz OCA], [http://pdbe.org/5iaz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iaz RCSB], [http://www.ebi.ac.uk/pdbsum/5iaz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iaz ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Most plant beta-galactosidases, which belong to glycoside hydrolase family 35, have a C-terminal domain homologous to animal galactose and rhamnose-binding lectins. To investigate the structure and function of this domain, the C-terminal domain of the rice (Oryza sativa L.) beta-galactosidase 1 (OsBGal1 Cter) was expressed in Escherichia coli and purified to homogeneity. The free OsBGal1 Cter is monomeric with a native molecular weight of 15kDa. NMR spectroscopy indicated that OsBGal1 Cter comprises five beta-strands and one alpha-helix. The structure of this domain is similar to lectin domains from animals, but loops A and C of OsBGal1 Cter are longer than the corresponding loops from related animal lectins with known structures. In addition, loop A of OsBGal1 Cter was not well defined, suggesting it is flexible. Although OsBGal1 Cter was predicted to be a galactose/rhamnose-binding domain, binding with rhamnose, galactose, glucose, beta-1,4-d-galactobiose and raffinose could not be observed in NMR experiments. | |||
Structure of a plant beta-galactosidase C-terminal domain.,Rimlumduan T, Hua YL, Tanaka T, Ketudat Cairns JR Biochim Biophys Acta. 2016 Jul 22;1864(10):1411-1418. doi:, 10.1016/j.bbapap.2016.07.005. PMID:27451952<ref>PMID:27451952</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Hua, Y | <div class="pdbe-citations 5iaz" style="background-color:#fffaf0;"></div> | ||
[[Category: Ketudat-Cairns, J | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hua, Y l]] | |||
[[Category: Ketudat-Cairns, J R]] | |||
[[Category: Rimlumduan, T]] | [[Category: Rimlumduan, T]] | ||
[[Category: Tanaka, T]] | [[Category: Tanaka, T]] | ||
[[Category: Beta-sandwich]] | |||
[[Category: Exoglycosidase]] | |||
[[Category: Glycoside hydrolase]] | |||
[[Category: Hydrolase]] | |||