5iaz: Difference between revisions

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New page: '''Unreleased structure''' The entry 5iaz is ON HOLD Authors: Rimlumduan, T., Hua, Y.-l., Tanaka, T., Ketudat-Cairns, J.R. Description: The C-terminal domain of rice beta-galactosidase...
 
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'''Unreleased structure'''


The entry 5iaz is ON HOLD
==The C-terminal domain of rice beta-galactosidase 1==
<StructureSection load='5iaz' size='340' side='right'caption='[[5iaz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5iaz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Indica_Group Oryza sativa Indica Group]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5IAZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5iaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iaz OCA], [https://pdbe.org/5iaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iaz RCSB], [https://www.ebi.ac.uk/pdbsum/5iaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iaz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B8ANX7_ORYSI B8ANX7_ORYSI]
<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.


Authors: Rimlumduan, T., Hua, Y.-l., Tanaka, T., Ketudat-Cairns, J.R.
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>


Description: The C-terminal domain of rice beta-galactosidase 1
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Hua, Y.-L]]
<div class="pdbe-citations 5iaz" style="background-color:#fffaf0;"></div>
[[Category: Ketudat-Cairns, J.R]]
 
[[Category: Rimlumduan, T]]
==See Also==
[[Category: Tanaka, T]]
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryza sativa Indica Group]]
[[Category: Hua Y-l]]
[[Category: Ketudat-Cairns JR]]
[[Category: Rimlumduan T]]
[[Category: Tanaka T]]

Latest revision as of 14:50, 6 November 2024

The C-terminal domain of rice beta-galactosidase 1The C-terminal domain of rice beta-galactosidase 1

Structural highlights

5iaz is a 1 chain structure with sequence from Oryza sativa Indica Group. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 25 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B8ANX7_ORYSI

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Rimlumduan T, Hua YL, Tanaka T, Ketudat Cairns JR. Structure of a plant beta-galactosidase C-terminal domain. Biochim Biophys Acta. 2016 Jul 22;1864(10):1411-1418. doi:, 10.1016/j.bbapap.2016.07.005. PMID:27451952 doi:http://dx.doi.org/10.1016/j.bbapap.2016.07.005
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