5iaz

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'''Unreleased structure'''
 
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The entry 5iaz is ON HOLD until Paper Publication
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==The C-terminal domain of rice beta-galactosidase 1==
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<StructureSection load='5iaz' size='340' side='right' caption='[[5iaz]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
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== Structural highlights ==
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<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>
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</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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Rimlumduan, T., Hua, Y.-l., Tanaka, T., Ketudat-Cairns, J.R.
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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>
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Description: The C-terminal domain of rice beta-galactosidase 1
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Hua, Y.-L]]
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<div class="pdbe-citations 5iaz" style="background-color:#fffaf0;"></div>
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[[Category: Ketudat-Cairns, J.R]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Hua, Y l]]
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[[Category: Ketudat-Cairns, J R]]
[[Category: Rimlumduan, T]]
[[Category: Rimlumduan, T]]
[[Category: Tanaka, T]]
[[Category: Tanaka, T]]
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[[Category: Beta-sandwich]]
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[[Category: Exoglycosidase]]
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[[Category: Glycoside hydrolase]]
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[[Category: Hydrolase]]

Revision as of 16:10, 10 August 2016

The C-terminal domain of rice beta-galactosidase 1

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