5e9a: Difference between revisions

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<StructureSection load='5e9a' size='340' side='right'caption='[[5e9a]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
<StructureSection load='5e9a' size='340' side='right'caption='[[5e9a]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5e9a]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Rahnella_sp._r3 Rahnella sp. r3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E9A OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5E9A FirstGlance]. <br>
<table><tr><td colspan='2'>[[5e9a]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rahnella_sp._R3 Rahnella sp. R3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5E9A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.561&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5e9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9a OCA], [http://pdbe.org/5e9a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e9a RCSB], [http://www.ebi.ac.uk/pdbsum/5e9a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e9a ProSAT]</span></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=5e9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e9a OCA], [https://pdbe.org/5e9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e9a RCSB], [https://www.ebi.ac.uk/pdbsum/5e9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e9a ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A0B4U8I5_9GAMM A0A0B4U8I5_9GAMM]
A novel gene was isolated for the first time from a psychrophilic gram-negative bacterium Rahnella sp. R3. The gene encoded a cold-adapted beta-galactosidase (R-beta-Gal). Recombinant R-beta-Gal was expressed in Escherichia coli BL21 (DE3), purified and characterized. R-beta-gal belongs to the glycosyl hydrolase family 42. Circular dichroism spectrometry of the structural stability of R-beta-Gal with respect to temperature indicated that the secondary structures of the enzyme were stable to 45 degrees C. In solution, the enzyme was a homo-trimer and was active at temperatures as low as 4 degrees C. The enzyme did not require the presence of metal ions to be active, but Mg(2+), Mn(2+), and Ca(2+) enhanced its activity slightly, whereas Fe(3+), Zn(2+) and Al(3+) appeared to inactive it. The purified enzyme displayed K(m) values of 6.5 mM for ONPG and 2.2mM for lactose at 4 degrees C. These values were lower than the corresponding K(m)s reported for other cold-adapted beta-Gals.
 
Cloning, expression and structural stability of a cold-adapted beta-galactosidase from Rahnella sp. R3.,Fan Y, Hua X, Zhang Y, Feng Y, Shen Q, Dong J, Zhao W, Zhang W, Jin Z, Yang R Protein Expr Purif. 2015 Nov;115:158-64. doi: 10.1016/j.pep.2015.07.001. Epub, 2015 Jul 3. PMID:26145832<ref>PMID:26145832</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5e9a" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
*[[Galactosidase 3D structures|Galactosidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beta-galactosidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rahnella sp. r3]]
[[Category: Rahnella sp. R3]]
[[Category: Fan, Y T]]
[[Category: Fan YT]]
[[Category: Zhang, Y Z]]
[[Category: Zhang YZ]]
[[Category: Galactosidase]]
[[Category: Hydrolase]]
[[Category: Lactose]]
[[Category: Tim barrel]]

Latest revision as of 15:27, 6 March 2024

Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3Crystal structure analysis of the cold-adamped beta-galactosidase from Rahnella sp. R3

Structural highlights

5e9a is a 6 chain structure with sequence from Rahnella sp. R3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.561Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0B4U8I5_9GAMM

See Also

5e9a, resolution 2.56Å

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